Affinage

RAD1

Cell cycle checkpoint protein RAD1 · UniProt O60671

Length
282 aa
Mass
31.8 kDa
Annotated
2026-06-10
100 papers in source corpus 51 papers cited in narrative 51 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAD1 is a conserved DNA repair and checkpoint protein that operates through two structurally and functionally distinct assemblies. In nucleotide excision repair and recombination, Rad1 partners with Rad10 to form a structure-specific endonuclease that degrades single-stranded DNA and cleaves duplex–single-strand junctions on the 3'-tailed strand (PMID:8479526, PMID:8091230); this activity generates 3'-hydroxyl/5'-phosphate termini and performs the 5' incision during NER, reconstituting dual incision when combined with XPG (PMID:8253764, PMID:7559571). Stable Rad1–Rad10 complex formation, mediated by conserved C-terminal hydrophobic domains, is essential for both repair and recombination, since an interaction-defective rad1 allele phenocopies the null (PMID:1518857, PMID:1620114). Genetically, Rad1-Rad10 is specifically required to remove nonhomologous 3' tails during single-strand annealing and gene-conversion DSB repair (PMID:1411547, PMID:7891718), to process 3'-blocked termini such as 3'-phosphoglycolate from oxidative breaks (PMID:15371342), and to repair Top1 cleavage complexes, with the catalytic-dead rad1-D869A mutant confirming the endonuclease requirement (PMID:12368472); targeting to lesions and substrates is provided by accessory factors including Rad14 in NER and Saw1 in SSA (PMID:16428464, PMID:23299942). In a second capacity, Rad1 is a subunit of the heterotrimeric 9-1-1 (Rad9-Hus1-Rad1) PCNA-like sliding clamp (PMID:11340080), whose toroidal ring architecture was confirmed crystallographically (PMID:19446481). Rad1 is essential for 9-1-1 integrity and for ATR-dependent (not ATM-dependent) Chk1 activation, with its loss destabilizing Rad9 and Hus1, causing radioresistant DNA synthesis and chromosomal abnormalities (PMID:15184880). The clamp is loaded onto damaged chromatin by Rad17 in a proximal, kinase-independent step (PMID:20110345, PMID:12228248) and activates Chk1 by positioning TopBP1's activation domain, recruited via CK2-phosphorylated Rad9, to stimulate ATR (PMID:17575048, PMID:20545769). Beyond signaling, 9-1-1 acts as a damage-specific scaffold that stimulates base excision repair enzymes including Pol β, FEN1, DNA ligase I, APE1, NEIL1, TDG and MYH through a repair-enzyme-binding site on the Rad1 IDC loop that is competitively blocked by p21 (PMID:19446481, PMID:19535328, PMID:15556996, PMID:16879101). The complex also localizes to telomeres and positively regulates telomerase (PMID:16890531), and contributes to meiotic chromosome surveillance (PMID:23468651, PMID:9716408).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1992 High

    Established that Rad1 and Rad10 form an obligate, salt-resistant complex and that this physical association is itself required for repair and recombination, defining Rad1's first functional context.

    Evidence Reciprocal Co-IP in vivo and in vitro plus an interaction-defective rad1 allele in yeast, with C-terminal domain mapping by truncation

    PMID:1518857 PMID:1620114

    Open questions at the time
    • Did not establish which subunit carries catalytic activity
    • Did not define substrate specificity of the complex
  2. 1992 High

    Placed Rad1 genetically at the 3'-end processing step of recombination, showing it removes nonhomologous tails during DSB repair.

    Evidence Genetic epistasis with HO-induced DSBs and Southern blot of recombination products in rad1 yeast

    PMID:1411547

    Open questions at the time
    • Biochemical mechanism of tail removal not yet demonstrated
    • Did not distinguish NER from recombination roles
  3. 1994 High

    Provided the biochemical basis for Rad1's repair and recombination roles by showing the complex cleaves at duplex–single-strand junctions on the 3'-tailed strand and produces clean termini, unifying the NER incision and tail-removal functions.

    Evidence In vitro cleavage of model recombination/repair intermediates and termini analysis with purified Rad1-Rad10

    PMID:8091230 PMID:8253764 PMID:8479526

    Open questions at the time
    • Catalytic subunit identity still ambiguous
    • In vivo lesion-targeting mechanism unaddressed
  4. 1995 High

    Reconstituted the NER dual incision step, demonstrating Rad1-Rad10 performs the 5' incision and cooperates with XPG, and reported failure to detect Holliday junction binding, conflicting with an earlier catalytic-subunit claim.

    Evidence In vitro bubble-substrate incision assay with purified Rad1-Rad10 and XPG; negative Holliday junction binding assay

    PMID:7559571 PMID:7935767

    Open questions at the time
    • Conflicting reports on Rad1-only Holliday junction activity unresolved
    • Substrate selection rules among related nucleases not yet defined
  5. 1995 High

    Showed the recombination role is specific to Rad1-Rad10 among NER factors, separating this sub-pathway from canonical NER.

    Evidence Genetic analysis of HO-induced DSB repair across multiple NER deletion strains with physical monitoring

    PMID:7891718

    Open questions at the time
    • Factors targeting the nuclease to recombination intermediates unknown
  6. 1998 Medium

    Identified human HRAD1 as the functional ortholog of fission yeast rad1+ with intrinsic nuclease activity and a checkpoint role, bridging yeast biochemistry to the mammalian checkpoint.

    Evidence Complementation of S. pombe rad1 mutants; recombinant 3'→5' exonuclease assay; nuclear localization and meiotic chromosome staining

    PMID:9660799 PMID:9716408

    Open questions at the time
    • Exonuclease activity from bacterial protein not validated in human cell context
    • Relationship of human nuclease activity to the 9-1-1 clamp role unclear
  7. 2001 High

    Defined Rad1's second context as a stable heterotrimeric 9-1-1 clamp and mapped intersubunit contacts, establishing the structural framework for checkpoint and BER functions.

    Evidence Reconstitution by co-expression, differential-tag Co-IP, size-exclusion chromatography of the human Rad9-Hus1-Rad1 complex

    PMID:10359610 PMID:11340080 PMID:9872989

    Open questions at the time
    • How the ring is loaded onto DNA not yet established
    • Functional output of the complex undefined at this stage
  8. 2002 Medium

    Showed 9-1-1 chromatin loading is a proximal, kinase- and replication-independent event, positioning the clamp upstream in the checkpoint cascade.

    Evidence Chromatin fractionation with kinase inhibitors and phospho-site mutants in human cells

    PMID:12228248

    Open questions at the time
    • Loading machinery not identified in this study
    • Direct DNA recognition determinants unaddressed
  9. 2004 High

    Established Rad1 as essential for 9-1-1 integrity and ATR-dependent (not ATM-dependent) Chk1 signaling, linking the clamp to genome stability phenotypes.

    Evidence siRNA knockdown of RAD1 with complex-stability blots, Chk1 phosphorylation, DNA fiber, and cytogenetic assays

    PMID:15184880

    Open questions at the time
    • Molecular intermediary between 9-1-1 and ATR not yet defined here
    • Distinct contributions of clamp vs nuclease roles to phenotypes not separated
  10. 2004 Medium

    Revealed a scaffolding function for 9-1-1 in base excision repair by showing it binds and stimulates specific BER enzymes (Pol β, FEN1) distinct from PCNA, broadening Rad1's role beyond signaling.

    Evidence In vitro pull-down and enzyme stimulation assays with purified 9-1-1 against multiple polymerases and substrates

    PMID:15314187 PMID:15556996

    Open questions at the time
    • Enzyme-binding surface on the clamp not yet localized
    • In vivo relevance of stimulation not directly tested
  11. 2007 High

    Defined the mechanism of 9-1-1-driven Chk1 activation: the clamp localizes TopBP1's activation domain via phospho-Rad9 to stimulate ATR, with this requirement bypassed by tethering the AD to other chromatin anchors.

    Evidence Co-IP, TopBP1-PCNA/H2B fusion bypass experiments, and phospho-Ser373 mutagenesis in human cells and Xenopus extracts

    PMID:17575048 PMID:17636252

    Open questions at the time
    • Kinase responsible for the activating Rad9 phosphorylation not identified here
    • Spatial coordination with the loader unresolved
  12. 2007 Medium

    Extended the BER scaffold role of 9-1-1 across multiple glycosylases and the AP-endonuclease/long-patch BER pathway, with several enzymes binding through the Rad1/Hus1 subunits.

    Evidence Co-IP, in vitro glycosylase/endonuclease stimulation, and LP-BER reconstitution for NEIL1, TDG, MYH and APE1

    PMID:16879101 PMID:17395641 PMID:17426133 PMID:17855402

    Open questions at the time
    • Whether all interactions occur simultaneously or competitively unresolved
    • In vivo BER contribution of clamp not quantified
  13. 2009 High

    Provided the crystallographic basis for damage-specific 9-1-1 function, locating the repair-enzyme-binding site on the Rad1 IDC loop and showing it is competed by p21, while the Rad9 tail regulates DNA binding.

    Evidence X-ray structures of human Rad9-Hus1-Rad1 with FEN1 PIP-box co-crystallization, p21 competition, and truncation DNA-binding assays

    PMID:19446481 PMID:19464297 PMID:19535328

    Open questions at the time
    • Structure of DNA-loaded clamp not resolved
    • Conformational basis of loader engagement not fully defined
  14. 2010 High

    Placed Rad17 mechanistically upstream of 9-1-1, showing ATP-dependent loading and CK2 phosphorylation of Rad9 are prerequisites for TopBP1 recruitment and checkpoint activation.

    Evidence Xenopus extract biochemistry with Rad17 ATPase mutants and chromatin fractionation; in vitro CK2 kinase assays with phospho-site mutants and UV/MMS sensitivity

    PMID:20110345 PMID:20545769

    Open questions at the time
    • Precise order of loading versus TopBP1 binding events partially inferred
    • Mammalian in vivo loading kinetics not directly measured
  15. 2013 High

    Identified accessory targeting factors and an alternative meiotic role for Rad1, showing Saw1 directs Rad1-Rad10 to 3'-tailed SSA substrates and that meiotic Rad1 localization can be 9-1-1-independent.

    Evidence Reconstituted cleavage with purified Rad1/Rad10 and Saw1, ChIP, and Co-IP; conditional Hus1 knockout mouse meiotic immunofluorescence

    PMID:18471978 PMID:23299942 PMID:23468651

    Open questions at the time
    • Molecular nature of 9-1-1-independent Rad1 meiotic function undefined
    • Whether human Rad1 uses a Saw1-like targeting factor unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the nuclease (Rad1-Rad10) and checkpoint-clamp (9-1-1) identities of Rad1 are coordinated within a single proteome, and the structural basis of conflicting Holliday-junction observations, remain open.
  • No study reconciles the dual structural assemblies of Rad1 in one system
  • Conflicting Holliday junction binding reports unresolved
  • In vivo separation of clamp vs nuclease contributions to mammalian phenotypes incomplete

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 7 GO:0140097 catalytic activity, acting on DNA 7 GO:0016787 hydrolase activity 5 GO:0060090 molecular adaptor activity 5 GO:0005198 structural molecule activity 3 GO:0003677 DNA binding 2
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 3 GO:0005694 chromosome 3
Pathway
R-HSA-73894 DNA Repair 6 R-HSA-8953897 Cellular responses to stimuli 4 R-HSA-1640170 Cell Cycle 3
Partners
FEN1HUS1RAD10RAD14RAD17RAD9SAW1TOPBP1
Complex memberships
9-1-1 (Rad9-Hus1-Rad1) clampRad1-Rad10 endonuclease

Evidence

Reading pass · 51 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1993 Purified yeast Rad1 and Rad10 proteins form a complex that possesses endonuclease activity specifically degrading single-stranded DNA by an endonucleolytic mechanism; this activity is presumed to remove non-homologous regions during mitotic recombination and to incise damaged DNA during nucleotide excision repair. In vitro biochemical assay with purified proteins; single-stranded DNA endonuclease activity reconstituted from purified Rad1 and Rad10 Nature High 8479526
1993 Purified yeast Rad1-Rad10 endonuclease activity on single-stranded and double-stranded DNA produces 3'-hydroxyl and 5'-phosphate termini; activity on double-stranded DNA is strongly dependent on negative superhelicity. In vitro biochemical characterization with purified Rad1 and Rad10 proteins; agarose gel electrophoresis and TCA precipitation assays The Journal of biological chemistry High 8253764
1994 Rad1-Rad10 complex cleaves model recombination/repair intermediates specifically at duplex-single-strand junctions, acting only on the strand containing the 3' single-stranded tail; this defines the biochemical basis for its role in removing nonhomologous tails during recombination and for 5' incision during NER. In vitro cleavage assay using model recombination and repair intermediate substrates with purified Rad1-Rad10 Science (New York, N.Y.) High 8091230
1994 Yeast Rad1 protein binds specifically to Holliday junctions and, in the presence of magnesium, catalyzes endonucleolytic cleavage of the junction independently of Rad10, identifying Rad1 as the catalytic subunit of the Rad1/Rad10 endonuclease. In vitro binding and cleavage assay with purified Rad1 protein and synthetic Holliday junction substrates Nature Medium 7935767
1995 Purified Rad1-Rad10 complex incises a synthetic bubble DNA substrate at the 5'-side of the centrally unpaired region; when combined with XPG, dual incisions at both ends of the bubble are observed, reconstituting the dual incision step of nucleotide excision repair in vitro. Separately, Rad1 failed to show interaction with synthetic Holliday junctions in this study (negative result). In vitro incision assay with purified Rad1-Rad10 and XPG on bubble DNA substrates; synthetic Holliday junction binding assay (negative) The Journal of biological chemistry High 7559571
1992 Yeast Rad1 and Rad10 proteins form a stable, specific complex in vitro and in vivo; the interaction is resistant to 1 M NaCl and low SDS; a rad1 mutant allele encoding a protein that fails to bind Rad10 is as defective in DNA repair and recombination as a null mutant, demonstrating that complex formation is essential for both biological activities. Co-immunoprecipitation from yeast cell extracts; in vitro co-translation and co-immunoprecipitation; mutational analysis (interaction-defective rad1 allele) Proceedings of the National Academy of Sciences of the United States of America High 1518857
1992 Stable and specific in vitro interaction between Rad1 and Rad10 proteins was mapped: the Rad10-binding domain of Rad1 maps to the C-terminal region, and the Rad1-binding domain of Rad10 also maps to its C-terminal region; these domains are evolutionarily conserved and hydrophobic. In vitro co-immunoprecipitation with in vitro translated proteins; domain mapping by truncation analysis Molecular and cellular biology High 1620114
1993 Rad1 and Rad10 form a constitutive complex in the cell nucleus; the Rad10-binding domain of Rad1 maps to amino acids 809–997, and the Rad1-binding domain of Rad10 maps to amino acids 90–210; these domains are hydrophobic and evolutionarily conserved. Yeast two-hybrid assay; domain mapping with truncation constructs Molecular microbiology Medium 8361362
1992 In Saccharomyces cerevisiae, Rad1 is required to remove nonhomologous DNA sequences (~60 bp) from the 3' ends of recombining DNA during double-strand break repair; recombination is restored when the ends are made homologous, placing Rad1 in the 3'-end processing step during single-strand annealing and gene conversion. Genetic epistasis using HO endonuclease-induced DSBs in rad1 mutant yeast; Southern blot analysis of recombination products Science (New York, N.Y.) High 1411547
1995 Among nucleotide excision repair genes, only RAD1 and RAD10 (not RAD2, RAD3, RAD14, RAD7, or RAD16) are required for removing nonhomologous sequences from DSB ends during gap repair and single-strand annealing, demonstrating a specific role for Rad1-Rad10 in this recombination sub-pathway. Genetic analysis of HO-induced DSB repair in multiple NER gene deletion strains; physical monitoring by Southern blot Molecular and cellular biology High 7891718
1999 Human hRad1 and hHus1 associate in a complex that interacts with a highly modified (phosphorylated) form of hRad9; hHus1 and hRad1 do not associate with hRad17; hRad9 is phosphorylated in response to DNA damage. Co-immunoprecipitation from human cell extracts; Western blotting The Journal of biological chemistry Medium 9872989
1999 Human hRAD9 physically associates with hRAD1 and hHUS1; hRAD1 and hHUS1 also interact with each other; hRAD9 is a nuclear phosphoprotein present in multiple phosphorylation forms in vivo. Co-immunoprecipitation from human cells; nuclear fractionation; Western blot Molecular biology of the cell Medium 10359610
2001 The human hRad9-hHus1-hRad1 (9-1-1) complex is a stable, discrete heterotrimeric complex of ~160 kDa in which: the N-terminus of hRad9 interacts with hRad1, the N-terminus of hRad1 interacts with hHus1, and the N-terminus of hHus1 interacts with the C-terminus of hRad9's PCNA-like region; approximately half the cellular hRad1 participates in this complex. Biochemical fractionation; reconstitution by co-expression in heterologous system; co-immunoprecipitation with differentially tagged proteins; size-exclusion chromatography The Journal of biological chemistry High 11340080
2000 Computational structure prediction indicates that human Rad1 (and its yeast/fission yeast orthologs) shares a PCNA-like fold; the three proteins Rad9, Hus1, and Rad1 are predicted to form a heterotrimeric PCNA-like ring, with a defined order within the ring and identified contact regions between subunits. Computational fold recognition, comparative modeling, and generalized sequence profiles; structural prediction validated against existing biochemical data Nucleic acids research Low 10871397
2009 Crystal structure of the human 9-1-1 (Rad9-Hus1-Rad1) complex reveals a toroidal PCNA-like heterotrimeric ring; the structure shows significant differences among the three subunits at sites implicated in clamp loader binding and ligand binding; biochemical analysis identifies a single repair enzyme-binding site on 9-1-1 that is competitively blocked by p21(cip1/waf1). X-ray crystallography; biochemical competition assay with p21 Molecular cell High 19446481
2009 Crystal structure of the human Rad9(1-272)-Hus1-Rad1 complex at 2.5 Å resolution confirms the closed toroidal architecture; co-crystallization reveals that an FEN1 PIP-box peptide binds to the interdomain connecting loop (IDC loop) of hRad1, providing the molecular basis for damage repair-specific activity of 9-1-1 distinct from PCNA. X-ray crystallography at 2.5 Å; co-crystallization with FEN1 PIP-box peptide; biochemical assays The Journal of biological chemistry High 19535328
2009 Crystal structure of human Rad9(1-272)-Hus1-Rad1 at 2.5 Å resolution shows the 9-1-1 complex forms a closed ring; the full-length 9-1-1 complex (with Rad9 C-terminal tail) does not form a stable complex with 5' recessed DNA, but the Rad9(1-272) truncation does, indicating that the C-terminal tail of Rad9 regulates DNA binding by 9-1-1. X-ray crystallography; DNA-binding assay comparing full-length and truncated 9-1-1 Journal of molecular biology High 19464297
2000 Human hRad17 interacts with the PCNA-like checkpoint proteins hRad1, hRad9, and hHus1 in a manner resembling the RFC–PCNA clamp loader interaction; DNA damage affects the association of hRad17 with the clamp-like proteins; mutational analysis of hRad1 and hRad17 confirms properties similar to RFC–PCNA interaction. Co-immunoprecipitation from human cells; mutational analysis of interaction surfaces; Western blot The Journal of biological chemistry Medium 10884395
2007 The 9-1-1 complex activates Chk1 via binding of Rad9's C-terminal tail to TopBP1, which then stimulates ATR-mediated Chk1 phosphorylation through TopBP1's activation domain (AD); fusion of the AD to PCNA or histone H2B bypasses the requirement for the 9-1-1 clamp, demonstrating that the primary role of 9-1-1 in Chk1 activation is to localize TopBP1's AD to stalled replication forks. Co-immunoprecipitation; TopBP1-PCNA and TopBP1-H2B fusion bypass experiments in human cells; Chk1 phosphorylation assays Genes & development High 17575048
2007 The 9-1-1 complex regulates the interaction of TopBP1 with ATR-ATRIP in Xenopus egg extracts; the BRCT I-II region of TopBP1 binds specifically to the 9-1-1 complex via the C-terminal domain of Rad9, and this interaction requires phosphorylation of Rad9 Ser-373; mutation of TopBP1 BRCT I-II or Rad9 Ser-373→Ala causes checkpoint defects. Co-immunoprecipitation from Xenopus egg extracts; checkpoint assays with mutant proteins; phospho-specific analysis The Journal of biological chemistry High 17636252
2010 Casein kinase 2 (CK2) phosphorylates Ser-341 and Ser-387 in the C-terminal tail of human Rad9; phosphorylation at these sites (particularly Ser-387) is required for the 9-1-1 complex to physically interact with TopBP1 and for efficient ATR-dependent checkpoint activation; cells expressing phospho-deficient Rad9 (S341A/S387A) are hypersensitive to UV and MMS. In vitro kinase assay with purified CK2 and 9-1-1; Co-IP; mutagenesis; UV/MMS sensitivity assays Genes to cells : devoted to molecular & cellular mechanisms High 20545769
2010 Rad17 mediates the interaction between 9-1-1 and TopBP1 in Xenopus egg extracts; ATP binding to Rad17 is essential for 9-1-1–TopBP1 association, and ATP hydrolysis by Rad17 is required for 9-1-1 loading onto DNA and for elevated TopBP1 chromatin accumulation; a 9-1-1 mutant unable to bind TopBP1 still promotes normal TopBP1 chromatin accumulation, placing Rad17 upstream. Xenopus egg extract biochemistry; Rad17 ATPase mutants; 9-1-1 TopBP1-binding mutant; chromatin fractionation assays Molecular biology of the cell High 20110345
2002 Genotoxin-induced chromatin association of the 9-1-1 complex does not require ATM, ATR, or DNA-PK catalytic activity, does not require Rad9 Ser-272 phosphorylation, and does not require DNA replication, establishing that 9-1-1 chromatin loading is a proximal, kinase-independent event in the checkpoint cascade. Chromatin fractionation assay in human cells with pharmacological kinase inhibitors and phospho-site mutants; flow cytometry The Journal of biological chemistry Medium 12228248
2004 Loss of RAD1 in mammalian cells destabilizes Rad9 and Hus1, causing disintegration of the 9-1-1 complex; Rad1 depletion impairs ATR-dependent (but not ATM-dependent) Chk1 activation, causes radioresistant DNA synthesis (RDS), and results in chromosomal abnormalities, establishing Rad1 as essential for ATR-dependent checkpoint signaling. siRNA knockdown of RAD1; Western blot for complex stability; Chk1 phosphorylation assays; DNA fiber assays; cytogenetics Oncogene High 15184880
2004 The human 9-1-1 complex physically interacts with DNA polymerase beta (Pol β) in vitro, stimulates its activity by increasing its affinity for the primer-template, and enhances strand displacement synthesis; 9-1-1 does not stimulate DNA polymerase lambda, alpha, or delta. In vitro pull-down; DNA polymerase activity assays with and without 9-1-1; primer extension assays Nucleic acids research Medium 15314187
2004 The human 9-1-1 complex binds and stimulates flap endonuclease 1 (FEN1) on flap, nick, and gapped substrates; stimulation requires 9-1-1 entry to the double-stranded region; 9-1-1 does not substitute for PCNA in stimulating DNA polymerase beta, making it a damage-specific FEN1 activator. In vitro FEN1 activity assay with purified 9-1-1; cleavage assays on multiple substrates Proceedings of the National Academy of Sciences of the United States of America High 15556996
2005 The human 9-1-1 complex interacts with and stimulates DNA ligase I; 9-1-1 improves the binding of DNA ligase I to nicked double-stranded DNA; UV irradiation stimulates 9-1-1–ligase I complex formation in cells; stimulation is specific for ligase I and does not require encirclement of the DNA substrate (unlike PCNA). Co-immunoprecipitation from human cells; in vitro ligation assay; UV irradiation stimulation experiment The Biochemical journal Medium 15871698
2006 The 9-1-1 complex stimulates DNA ligase I by improving its binding to nicked DNA; high concentrations of casein kinase II inhibit ligase I but do not prevent 9-1-1-mediated stimulation; unlike PCNA, 9-1-1 stimulates DNA ligase I equally on linear and circular substrates, indicating encirclement is not required. In vitro ligation assay; DNA binding assay; kinase inhibition experiment The Journal of biological chemistry Medium 16731526
2006 Human MYH DNA glycosylase interacts with hRad1 and hHus1 (but not hRad9) of the 9-1-1 complex; the major interaction site maps to residues 295–350 of hMYH; hHus1 and the 9-1-1 complex enhance MYH glycosylase activity; the hMYH-hHus1 interaction is enhanced after ionizing radiation. Co-immunoprecipitation; in vitro pulldown; glycosylase activity assay with and without 9-1-1; mutagenesis of interaction sites The Biochemical journal Medium 16879101
2007 The human 9-1-1 complex interacts with hNEIL1 DNA glycosylase; residues 290–350 of hNEIL1 are important for 9-1-1 association; hHus1, hRad1, and hRad9 individually and as a complex significantly stimulate hNEIL1 glycosylase activity; a fraction of hNEIL1 nuclear foci co-localizes with hRad9 foci after hydrogen peroxide treatment. Co-immunoprecipitation; in vitro glycosylase stimulation assay; immunofluorescence co-localization Nucleic acids research Medium 17395641
2007 The human 9-1-1 complex interacts with thymine DNA glycosylase (hTDG); hHus1 interacting domain maps to residues 67–110 of hTDG (Val74 critical); hHus1, hRad1, hRad9 individually and as a complex stimulate hTDG glycosylase activity; the hRad9-hTDG interaction is enhanced after MNNG treatment. Co-immunoprecipitation; mutagenesis; in vitro glycosylase activity assay; immunofluorescence Nucleic acids research Medium 17855402
2007 The 9-1-1 complex interacts with APE1 in vitro and in vivo, stimulates APE1 AP-endonuclease activity, and stimulates long-patch base excision repair (LP-BER) reconstituted in vitro by specifically enhancing the activities of APE1 and Pol β as early LP-BER components. Co-immunoprecipitation; in vitro AP-endonuclease assay; LP-BER reconstitution assay Nucleic acids research Medium 17426133
2005 The 9-1-1 complex independently binds and activates FEN1, and this stimulation is abolished by acetylation of FEN1 by p300-HAT, whereas PCNA stimulation of FEN1 is unaffected by acetylation, suggesting independent regulatory mechanisms for the two clamps. In vitro FEN1 activity assay; p300-mediated acetylation of FEN1; comparison with PCNA stimulation Journal of molecular biology Medium 16216273
2005 The 9-1-1 complex directly interacts with RPA in human cells; this interaction is mediated by Rad9 binding to RPA70 and RPA32 subunits; UV or camptothecin treatment stimulates 9-1-1–RPA interaction; RPA knockdown by siRNA blocks damage-dependent chromatin association of 9-1-1 and also inhibits 9-1-1 complex formation. Co-immunoprecipitation; siRNA knockdown; immunofluorescence co-localization; chromatin fractionation Oncogene Medium 15897895
2004 In Schizosaccharomyces pombe, Hus1 associates in a complex with Rad9 and Rad1; this Rad1-Rad9-Hus1 complex is detectable in soluble extracts; nuclear localization of Hus1 depends on Rad17; Rad17 forms a separate complex in soluble extracts distinct from the Rad1-Rad9-Hus1 complex but shows transient interaction with Rad1. Immunoprecipitation from S. pombe extracts; indirect immunofluorescence; two-hybrid assay; in vitro association Molecular and cellular biology Medium 10648611
1996 Mismatch repair genes MSH2 and MSH3 function in the RAD1-RAD10 recombination pathway in yeast; msh3Δ has an effect similar to rad1Δ and rad10Δ on recombination between his3 duplications and homologous integration; epistasis analysis places MSH2 and MSH3 in the RAD1-RAD10 pathway. Genetic epistasis analysis; recombination frequency measurement in single and double mutants Genetics Medium 8849883
2003 Yeast Rad1 (with Mre11 and Rad50) defines a Ku-independent microhomology-mediated end joining (MMEJ) pathway for repairing DSBs lacking complementary end sequences; this MMEJ produces deletions annealed by ~8–10 bp microhomology at junctions and is Ku-independent but strongly dependent on Mre11, Rad50, and Rad1. Genetic analysis with HO-induced DSBs in yku70Δ rad1Δ and mre11Δ mutants; Southern blot analysis of repair products Molecular and cellular biology Medium 14612421
2002 The yeast Rad1-Rad10 structure-specific endonuclease and tyrosyl-DNA phosphodiesterase Tdp1 function as primary redundant pathways for repairing Top1 replicative damage (Top1 cleavage complexes); the catalytic point mutant rad1-D869A (Rad1-Rad10 nuclease-dead) is as sensitive as rad1Δ, confirming endonuclease activity is required; the Rad1-Rad10 pathway depends on RAD52, RAD51, RAD50, RAD59, and SRS2 but is independent of other NER genes. Genetic analysis with camptothecin sensitivity; use of catalytic point mutant rad1-D869A; epistasis with multiple recombination genes Proceedings of the National Academy of Sciences of the United States of America High 12368472
2004 Yeast Rad1-Rad10 nuclease is required for removing 3'-blocked termini (including 3'-phosphoglycolate) from DNA strand breaks induced by H2O2; Rad1-Rad10 in vitro efficiently cleaves DNA modified with a 3'-phosphoglycolate terminus; the nuclease acts redundantly with Apn1 and Apn2 in this 3'-end processing pathway. In vitro cleavage assay with 3'-phosphoglycolate-modified substrates; genetic analysis (apn1 apn2 rad1 triple mutants); H2O2 sensitivity experiments Genes & development High 15371342
2006 Complex formation between Rad1-Rad10 nuclease and the damage recognition protein Rad14 is essential for Rad1-Rad10 to function in NER in vivo; two rad1 mutations were identified that render cells as UV-sensitive as rad1Δ but do not affect Rad1's recombination function, and these mutations abolish Rad14 interaction without affecting Rad10 interaction, establishing that Rad14 binding provides damage-site targeting for Rad1-Rad10. Mutational analysis of RAD1; in vivo UV sensitivity; biochemical complex formation assays; separation-of-function mutants Molecular and cellular biology High 16428464
2008 Saw1 (Yal027Wp) is required for Rad1/Rad10-dependent 3' flap cleavage during single-strand annealing (SSA); Saw1 physically interacts with Rad1/Rad10, Msh2/Msh3, and Rad52; Saw1 mutants that fail to interact with Rad1 but retain Rad52/Msh2 interaction are specifically defective in 3' flap removal; deletion of SAW1 abolishes association of Rad1 at SSA intermediates in vivo. Microarray-based genetic screen; Co-IP; physical interaction mapping; chromatin immunoprecipitation (ChIP); SSA assay Molecular cell High 18471978
2010 Mec1/Tel1-dependent phosphorylation of Slx4 at Thr113 is required for efficient cleavage of 3' non-homologous DNA tails by Rad1-Rad10 during single-strand annealing and homologous recombination; Slx4 is recruited to 3' NH tails during DSB repair independently of its phosphorylation; deletion of both MEC1 and TEL1 severely reduces NH tail cleavage. Genetic analysis; site-directed mutagenesis of Slx4 phosphorylation sites; ChIP; SSA assay DNA repair Medium 20382573
2013 Saw1 is a structure-specific DNA binding protein with high affinity for splayed arm and 3'-flap DNAs; Saw1 physically interacts with Rad1 and facilitates targeting of Rad1 to 3'-tailed substrates in vivo and in vitro; Saw1 enhances 3'-tail cleavage by Rad1/Rad10 in a purified reconstituted system. In vitro DNA binding assay; in vitro cleavage assay with purified Rad1/Rad10 and Saw1; ChIP; Co-IP The EMBO journal High 23299942
2003 In fission yeast, damage-induced Crb2 (Rad9/53BP1 homolog) nuclear foci form independently of Rad1, Rad3, and Rad17 complexes, but these complexes are required for persistent (long-lasting) retention of Crb2 at DSB sites, placing the 9-1-1/Rad3 complexes in the retention rather than initial recruitment of Crb2. Live-cell fluorescence microscopy of Crb2-GFP in rad1, rad3, rad17 mutants; time-course analysis of foci persistence Molecular and cellular biology Medium 12917337
2003 Mus81-Mms4 and Rad1-Rad10 are homologous structure-specific endonucleases with distinct cleavage site selection: Rad1-Rad10 cleavage site is determined by the branch point, while Mus81-Mms4 cleavage is determined by the 5' end of the strand at the flap junction; substrates lacking a 5' end near the flap are cleaved poorly by Mus81-Mms4 but well by Rad1-Rad10. In vitro cleavage assay with defined substrates comparing Mus81-Mms4 and Rad1-Rad10 endonucleases Molecular and cellular biology High 12724407
2012 The Rad1-Rad10 nuclease promotes crossover and non-crossover recombinants between ectopic sequences; crossover products are absent only from the mus81Δ rad1Δ yen1Δ triple mutant, indicating that Rad1-Rad10 participates with Mus81-Mms4 and Yen1 in processing recombination intermediates between dispersed repeats; Rad1-dependent joint molecules accumulate in mus81Δ yen1Δ mutants. Genetic analysis; physical monitoring of recombination intermediates by Southern blot; triple mutant analysis Nature structural & molecular biology Medium 22885325
2013 In mouse testis, HUS1 loss (in 9-1-1) causes persistent meiotic DSBs, synapsis defects, and spermatocyte depletion; RAD9 localizes to RAD51-containing foci in a HUS1-dependent manner; RAD1 has a broader meiotic chromosome distribution that only partially overlaps with RAD9, and RAD1 localization to the XY body and unsynapsed autosomes is HUS1-independent, suggesting RAD1 can function through an alternative mechanism outside the canonical 9-1-1 complex. Conditional Hus1 knockout in mouse testis; immunofluorescence of meiotic chromosome spreads; phenotypic analysis PLoS genetics Medium 23468651
1998 Human HRAD1 (HisHrad1A) has 3'→5' exonuclease activity when expressed and purified from bacteria; the shorter splice variant HisHrad1B lacks this activity; HRAD1 is located on chromosome 5p13.2-13.3. Recombinant protein expression and purification; in vitro exonuclease assay The Journal of biological chemistry Medium 9660799
1998 Human HRAD1 complements UV sensitivity and G2 checkpoint defects of S. pombe rad1 mutants, establishing that HRAD1 is the functional human ortholog of S. pombe rad1+; HRAD1 protein localizes predominantly to the nucleus and is expressed at high levels in proliferative tissues; mouse Rad1 is associated with meiotic chromosomes during spermatogenesis prophase I. Complementation assay in S. pombe rad1 mutant; nuclear localization by immunofluorescence; meiotic chromosome spread immunostaining Genes & development Medium 9716408
2006 The mammalian 9-1-1 complex localizes to telomeres in human and mouse cells; HUS1-deficient mouse fibroblasts and thymocytes show severe telomere shortening; 9-1-1 associates with catalytically competent telomerase in cell lysates and acts as a positive regulator of telomerase DNA polymerase activity. Chromatin immunoprecipitation at telomeres; telomere length measurement (Q-FISH and Southern); Co-IP with telomerase; telomerase activity assay Current biology : CB Medium 16890531
2004 hRad9, hHus1, and hRad1 (9-1-1 complex) localize as constitutive components of ALT-associated PML bodies (APBs) in ALT cells, colocalizing with telomeric DNA and γ-H2AX; this places the 9-1-1 complex at telomeric DSBs in ALT cells. Immunofluorescence and FISH co-localization; ChIP at telomeres The Journal of biological chemistry Medium 15075340

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 The Rad9-Hus1-Rad1 (9-1-1) clamp activates checkpoint signaling via TopBP1. Genes & development 388 17575048
1992 Removal of nonhomologous DNA ends in double-strand break recombination: the role of the yeast ultraviolet repair gene RAD1. Science (New York, N.Y.) 324 1411547
2003 Yeast Mre11 and Rad1 proteins define a Ku-independent mechanism to repair double-strand breaks lacking overlapping end sequences. Molecular and cellular biology 285 14612421
2004 Dial 9-1-1 for DNA damage: the Rad9-Hus1-Rad1 (9-1-1) clamp complex. DNA repair 257 15279787
1994 Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease. Science (New York, N.Y.) 247 8091230
2007 The Rad9-Hus1-Rad1 checkpoint clamp regulates interaction of TopBP1 with ATR. The Journal of biological chemistry 232 17636252
1989 The genetic control of direct-repeat recombination in Saccharomyces: the effect of rad52 and rad1 on mitotic recombination at GAL10, a transcriptionally regulated gene. Genetics 230 2693208
2000 Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic acids research 217 10871397
1992 Checkpoint controls in Schizosaccharomyces pombe: rad1. The EMBO journal 215 1563349
2000 Characterization of Schizosaccharomyces pombe Hus1: a PCNA-related protein that associates with Rad1 and Rad9. Molecular and cellular biology 202 10648611
1988 RAD1, an excision repair gene of Saccharomyces cerevisiae, is also involved in recombination. Molecular and cellular biology 202 3065620
1995 RAD1 and RAD10, but not other excision repair genes, are required for double-strand break-induced recombination in Saccharomyces cerevisiae. Molecular and cellular biology 190 7891718
2002 Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage. Proceedings of the National Academy of Sciences of the United States of America 183 12368472
1993 Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease. Nature 183 8479526
1999 Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. The Journal of biological chemistry 168 9872989
2003 The mechanism of Mus81-Mms4 cleavage site selection distinguishes it from the homologous endonuclease Rad1-Rad10. Molecular and cellular biology 159 12724407
1988 Different types of recombination events are controlled by the RAD1 and RAD52 genes of Saccharomyces cerevisiae. Genetics 138 3058548
1995 The Drosophila meiotic recombination gene mei-9 encodes a homologue of the yeast excision repair protein Rad1. Genetics 136 8647398
1990 RAD10, an excision repair gene of Saccharomyces cerevisiae, is involved in the RAD1 pathway of mitotic recombination. Molecular and cellular biology 135 2188090
1999 The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1. Molecular biology of the cell 117 10359610
1995 Role of reciprocal exchange, one-ended invasion crossover and single-strand annealing on inverted and direct repeat recombination in yeast: different requirements for the RAD1, RAD10, and RAD52 genes. Genetics 116 7705617
2001 Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage responsive checkpoint complex. The Journal of biological chemistry 114 11340080
1996 Requirement of mismatch repair genes MSH2 and MSH3 in the RAD1-RAD10 pathway of mitotic recombination in Saccharomyces cerevisiae. Genetics 114 8849883
1986 Homologous pairing of DNA molecules by Ustilago rec1 protein is promoted by sequences of Z-DNA. Cell 113 3948243
1995 Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination. The Journal of biological chemistry 109 7559571
2004 The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair. Nucleic acids research 103 15314187
2002 Endogenous DNA abasic sites cause cell death in the absence of Apn1, Apn2 and Rad1/Rad10 in Saccharomyces cerevisiae. The EMBO journal 103 12032096
2009 Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation. Molecular cell 102 19446481
1993 Purification and characterization of the Saccharomyces cerevisiae RAD1/RAD10 endonuclease. The Journal of biological chemistry 102 8253764
2004 ATR, Claspin and the Rad9-Rad1-Hus1 complex regulate Chk1 and Cdc25A in the absence of DNA damage. Cell cycle (Georgetown, Tex.) 101 15190204
1989 Yeast intrachromosomal recombination: long gene conversion tracts are preferentially associated with reciprocal exchange and require the RAD1 and RAD3 gene products. Genetics 99 2558957
1985 Left-handed DNA and the synaptic pairing reaction promoted by Ustilago rec1 protein. Cell 98 3967291
2005 Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells. Oncogene 93 15897895
2004 Localization of hRad9, hHus1, hRad1, and hRad17 and caffeine-sensitive DNA replication at the alternative lengthening of telomeres-associated promyelocytic leukemia body. The Journal of biological chemistry 92 15075340
1994 Specificity of the yeast rev3 delta antimutator and REV3 dependency of the mutator resulting from a defect (rad1 delta) in nucleotide excision repair. Genetics 92 8088509
1998 A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease. The Journal of biological chemistry 91 9660799
2003 X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes. Structure (London, England : 1993) 90 12679022
1998 Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis. Genes & development 89 9716408
2004 The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1. Proceedings of the National Academy of Sciences of the United States of America 88 15556996
2003 Retention but not recruitment of Crb2 at double-strand breaks requires Rad1 and Rad3 complexes. Molecular and cellular biology 85 12917337
2000 The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. The Journal of biological chemistry 85 10884395
1999 Dependence on RAD52 and RAD1 for anticancer drug resistance mediated by inactivation of mismatch repair genes. Current biology : CB 85 9889125
1984 Synapsis promoted by Ustilago rec1 protein. Cell 85 6321036
1992 Stable and specific association between the yeast recombination and DNA repair proteins RAD1 and RAD10 in vitro. Molecular and cellular biology 83 1620114
2006 Physical and functional interactions between MutY glycosylase homologue (MYH) and checkpoint proteins Rad9-Rad1-Hus1. The Biochemical journal 82 16879101
1994 Unrepaired heteroduplex DNA in Saccharomyces cerevisiae is decreased in RAD1 RAD52-independent recombination. Genetics 82 8070653
1993 Replication-dependent sister chromatid recombination in rad1 mutants of Saccharomyces cerevisiae. Genetics 78 8454200
2008 Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates. Molecular cell 77 18471978
1992 Specific complex formation between proteins encoded by the yeast DNA repair and recombination genes RAD1 and RAD10. Proceedings of the National Academy of Sciences of the United States of America 77 1518857
1994 The rad16 gene of Schizosaccharomyces pombe: a homolog of the RAD1 gene of Saccharomyces cerevisiae. Molecular and cellular biology 74 8114734
2009 Structure and functional implications of the human rad9-hus1-rad1 cell cycle checkpoint complex. The Journal of biological chemistry 71 19535328
2004 Interaction of checkpoint proteins Hus1/Rad1/Rad9 with DNA base excision repair enzyme MutY homolog in fission yeast, Schizosaccharomyces pombe. The Journal of biological chemistry 70 15533944
2002 Genotoxin-induced Rad9-Hus1-Rad1 (9-1-1) chromatin association is an early checkpoint signaling event. The Journal of biological chemistry 66 12228248
2007 The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylase. Nucleic acids research 65 17395641
2009 Crystal structure of the human rad9-hus1-rad1 clamp. Journal of molecular biology 63 19464297
2007 The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta in long patch base excision repair. Nucleic acids research 61 17426133
1999 Removal of one nonhomologous DNA end during gene conversion by a RAD1- and MSH2-independent pathway. Genetics 61 10101166
2005 The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery. The Biochemical journal 60 15871698
2005 The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity. Journal of molecular biology 60 16216273
1995 Mutant rec-1 eliminates the meiotic pattern of crossing over in Caenorhabditis elegans. Genetics 60 8601478
2004 Disruption of the Rad9/Rad1/Hus1 (9-1-1) complex leads to checkpoint signaling and replication defects. Oncogene 59 15184880
2012 Distinct roles of Mus81, Yen1, Slx1-Slx4, and Rad1 nucleases in the repair of replication-born double-strand breaks by sister chromatid exchange. Molecular and cellular biology 58 22354996
2010 Rad17 plays a central role in establishment of the interaction between TopBP1 and the Rad9-Hus1-Rad1 complex at stalled replication forks. Molecular biology of the cell 57 20110345
1990 Cloning and analysis of a gene involved in DNA repair and recombination, the rad1 gene of Schizosaccharomyces pombe. Molecular and cellular biology 56 2355921
2010 A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions. Journal of molecular biology 55 20816984
2007 The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase. Nucleic acids research 55 17855402
1994 The REC1 gene of Ustilago maydis involved in the cellular response to DNA damage encodes an exonuclease. The Journal of biological chemistry 55 8276878
1993 Yeast DNA recombination and repair proteins Rad1 and Rad10 constitute a complex in vivo mediated by localized hydrophobic domains. Molecular microbiology 54 8361362
2013 Conditional inactivation of the DNA damage response gene Hus1 in mouse testis reveals separable roles for components of the RAD9-RAD1-HUS1 complex in meiotic chromosome maintenance. PLoS genetics 50 23468651
2003 Multiple recombination pathways for sister chromatid exchange in Saccharomyces cerevisiae: role of RAD1 and the RAD52 epistasis group genes. Nucleic acids research 50 12736307
1992 Genome rearrangement in top3 mutants of Saccharomyces cerevisiae requires a functional RAD1 excision repair gene. Molecular and cellular biology 49 1328869
2012 Repair complexes of FEN1 endonuclease, DNA, and Rad9-Hus1-Rad1 are distinguished from their PCNA counterparts by functionally important stability. Proceedings of the National Academy of Sciences of the United States of America 48 22586102
2010 A pH-responsive interface derived from resilin-mimetic protein Rec1-resilin. Biomaterials 48 20223516
2010 Mec1/Tel1-dependent phosphorylation of Slx4 stimulates Rad1-Rad10-dependent cleavage of non-homologous DNA tails. DNA repair 48 20382573
2005 Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms. Structure (London, England : 1993) 47 16084390
2004 Requirement of yeast Rad1-Rad10 nuclease for the removal of 3'-blocked termini from DNA strand breaks induced by reactive oxygen species. Genes & development 47 15371342
1990 Specificity of the mutator effect caused by disruption of the RAD1 excision repair gene of Saccharomyces cerevisiae. Journal of bacteriology 46 2160935
2006 Mechanism of stimulation of human DNA ligase I by the Rad9-rad1-Hus1 checkpoint complex. The Journal of biological chemistry 45 16731526
1987 Nucleotide sequence and functional analysis of the RAD1 gene of Saccharomyces cerevisiae. Molecular and cellular biology 45 3550428
2006 Telomere and telomerase modulation by the mammalian Rad9/Rad1/Hus1 DNA-damage-checkpoint complex. Current biology : CB 44 16890531
1994 Holliday junction cleavage by yeast Rad1 protein. Nature 44 7935767
1998 cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster. Genomics 43 9878245
2006 Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivo. Molecular and cellular biology 42 16428464
1984 Molecular cloning and nucleotide sequence analysis of the Saccharomyces cerevisiae RAD1 gene. Molecular and cellular biology 42 6095044
2015 SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9-Rad1-Hus1 checkpoint clamp. BMC molecular biology 41 26063178
2012 The Rad1-Rad10 nuclease promotes chromosome translocations between dispersed repeats. Nature structural & molecular biology 41 22885325
2001 Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complex. Molecular biology of the cell 40 11739777
1983 Molecular cloning and characterization of the RAD1 gene of Saccharomyces cerevisiae. Gene 39 6368317
2010 Casein kinase 2-dependent phosphorylation of human Rad9 mediates the interaction between human Rad9-Hus1-Rad1 complex and TopBP1. Genes to cells : devoted to molecular & cellular mechanisms 38 20545769
2003 The role of yeast DNA 3'-phosphatase Tpp1 and rad1/Rad10 endonuclease in processing spontaneous and induced base lesions. The Journal of biological chemistry 37 12783866
1996 Homologous and homeologous intermolecular gene conversion are not differentially affected by mutations in the DNA damage or the mismatch repair genes RAD1, RAD50, RAD51, RAD52, RAD54, PMS1 and MSH2. Genetics 37 8725224
2013 Role of Saw1 in Rad1/Rad10 complex assembly at recombination intermediates in budding yeast. The EMBO journal 35 23299942
2015 Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin. Scientific reports 34 26042819
1996 Cloning, characterization, and chromosomal localization of rec1.3, a member of the G-protein-coupled receptor family highly expressed in brain. Brain research. Molecular brain research 34 9013780
1985 Reexamination of phenotypic defects in rec-1 and rec-2 mutants of Haemophilus influenzae Rd. Journal of bacteriology 34 3874865
2014 Interaction between Rad9-Hus1-Rad1 and TopBP1 activates ATR-ATRIP and promotes TopBP1 recruitment to sites of UV-damage. DNA repair 33 25091155
1998 HRAD1 and MRAD1 encode mammalian homologues of the fission yeast rad1(+) cell cycle checkpoint control gene. Nucleic acids research 33 9705507
2017 The Medicago truncatula GRAS protein RAD1 supports arbuscular mycorrhiza symbiosis and Phytophthora palmivora susceptibility. Journal of experimental botany 32 29186498
2011 Self-organization, interfacial interaction and photophysical properties of gold nanoparticle complexes derived from resilin-mimetic fluorescent protein rec1-resilin. Biomaterials 32 21295342
2010 Mouse Rad1 deletion enhances susceptibility for skin tumor development. Molecular cancer 32 20334655

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