Affinage

RRP1

Ribosomal RNA processing protein 1 homolog A · UniProt P56182

Length
461 aa
Mass
52.8 kDa
Annotated
2026-06-10
32 papers in source corpus 21 papers cited in narrative 20 extracted findings
Cross-family judge faithfulness: 6/7 claims corpus-supported (86%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

The RRP1 symbol in this corpus maps to several distinct, organism-specific proteins, and the timeline fragments accordingly. In human cells, RRP1 (Nop52/NNP-1) is a nucleolar factor of early ribosome biogenesis: it localizes to the granular component and dense fibrillar component of the nucleolus in an RNA Pol I transcription-dependent manner and is recruited late during post-mitotic nucleologenesis (PMID:10341208, PMID:25969445). It is a component of the 90S pre-ribosomal particle and is required for site 2 cleavage within ITS1 of 47S/45S, 41S, and 36S pre-rRNAs, acting in concert with XRN2 to accelerate this cleavage (PMID:25969445). RRP1 directly binds p32 (C1QBP) and competes with fibrillarin for this interaction, a competitive exchange that drives remodeling of pre-90S particles into pre-40S and pre-60S (PMID:21536856). The orthologous yeast RRP1 genes perform analogous roles in large-subunit rRNA maturation: S. cerevisiae Rrp1p is a nucleolar protein of 66S pre-ribosomal particles whose inactivation blocks 27SA3 and 27SB pre-rRNA processing toward mature 25S/5.8S rRNA (PMID:3549696, PMID:15100437). A separate human function has been defined in inflammatory macrophages, where RRP1 acts as an mRNA-binding post-transcriptional suppressor of TYMS, restraining folate/one-carbon metabolism and innate inflammation; myeloid-specific RRP1 loss produces severe experimental arthritis (PMID:40715096). The Drosophila protein bearing the Rrp1 name is mechanistically unrelated: it is a class II AP endonuclease with associated 3'-exonuclease, 3'-phosphodiesterase, 3'-phosphatase, and DNA strand transfer activities, all dependent on a C-terminal exonuclease III-homology domain (with Glu-461 essential for catalysis), and it protects against oxidative DNA damage in vivo and serves as a redox regulator of long-term memory (PMID:1713691, PMID:7692963, PMID:7798276, PMID:8643678, PMID:41289397). The S. pombe Rrp1 is yet another distinct protein — a Rad5/16-like SWI2/SNF2 translocase and Rad51-targeting E3 ubiquitin ligase acting in homologous recombination and centromeric nucleosome dynamics (PMID:34157114, PMID:23828040). These activities should not be conflated into a single protein; the timeline describes name-sharing factors across species rather than one conserved enzyme.

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1987 Medium

    Established that a gene named RRP1 is required for ribosomal RNA maturation, defining the founding ribosome-biogenesis function of the yeast gene.

    Evidence Temperature-sensitive mutant analysis and RNA processing assays in S. cerevisiae

    PMID:3549696

    Open questions at the time
    • Did not define the molecular activity of Rrp1p
    • No physical association with pre-ribosomes shown at this stage
  2. 1990 Medium

    Genetic suppressor screening implicated a partner gene (SRD1) functionally interacting with yeast RRP1, framing RRP1 within a regulatable processing pathway.

    Evidence Second-site suppressor screen with allele-specificity test in S. cerevisiae

    PMID:2179050

    Open questions at the time
    • No direct physical interaction demonstrated between SRD1 and RRP1 products
    • Molecular mechanism of suppression unknown
  3. 1991 High

    Resolved that the Drosophila protein named Rrp1 is a multifunctional DNA repair enzyme, assigning AP endonuclease, 3'-exonuclease, ssDNA renaturation, and strand transfer activities to defined domains.

    Evidence Protein purification from embryo extracts, in vitro enzymatic assays, domain dissection, and trans-complementation with E. coli exonuclease III

    PMID:1653418 PMID:1713691 PMID:7678415

    Open questions at the time
    • No structure of the full-length protein
    • Physiological substrate in vivo not yet defined
  4. 1993 High

    Defined the Drosophila Rrp1 cleavage chemistry and demonstrated it functions in cellular DNA repair, establishing it as a class II AP endonuclease active in vivo.

    Evidence In vitro endonuclease assays with defined abasic substrates plus complementation of repair-deficient E. coli (xth nfo) with damage-survival assays

    PMID:7692963 PMID:7694234

    Open questions at the time
    • Endogenous Drosophila phenotype of Rrp1 loss not addressed
    • Did not distinguish oxidative versus alkylation lesion preference
  5. 1994 High

    Active-site mutagenesis identified catalytic and specificity-determining residues and uncovered separable handling of alkylation versus oxidative lesions by Drosophila Rrp1.

    Evidence Site-directed mutagenesis (Glu-461, Thr-462, Lys-463) with E. coli complementation and in vitro nuclease assays

    PMID:7798276

    Open questions at the time
    • Structural basis of lesion discrimination not resolved
    • No in vivo Drosophila validation of residue requirements
  6. 1995 High

    Extended the Drosophila Rrp1 activity repertoire to 3'-end cleanup, showing it removes oxidative 3'-blocking groups to generate primer-ready termini.

    Evidence In vitro assays with site-specifically damaged oligonucleotides bearing 3'-phosphoglycolate and 3'-phosphate termini

    PMID:7530050

    Open questions at the time
    • Relative in vivo contribution of each activity unknown
    • No coupling to downstream repair polymerase/ligase demonstrated
  7. 1996 High

    Demonstrated a lesion-specific in vivo repair role for Drosophila Rrp1 and characterized sequence dependence of its exonuclease, linking biochemistry to genome protection.

    Evidence Drosophila mosaic eye loss-of-heterozygosity assay with inducible transgene overexpression, plus in vitro exonuclease sequence-preference assays

    PMID:8643678 PMID:8918793

    Open questions at the time
    • Loss-of-function (rather than overexpression) phenotype not tested
    • Endogenous expression and regulation not characterized
  8. 1998 Medium

    Defined the bipartite architecture of Drosophila Rrp1, mapping catalytic activities to a folded C-terminal exonuclease III-homology domain and assigning a disordered N-terminus.

    Evidence Limited proteolysis, circular dichroism, frictional analysis, and enzymatic assays of isolated domains

    PMID:9852053

    Open questions at the time
    • No high-resolution crystal structure
    • Function of the disordered N-terminal region beyond strand transfer unresolved
  9. 1999 High

    Identified human RRP1 (Nop52/NNP-1) as a nucleolar protein of late rRNA processing, placing the human gene in ribosome biogenesis rather than DNA repair.

    Evidence Immunocytochemistry with autoantibodies, cDNA transfection, cell-cycle and colocalization analysis with hPop1 and B23 in human cells

    PMID:10341208

    Open questions at the time
    • No direct rRNA-processing function demonstrated yet
    • Molecular activity of human RRP1 undefined at this stage
  10. 2004 High

    Established yeast Rrp1p as a 66S pre-ribosomal particle component and pinpointed the specific pre-rRNA processing steps it controls.

    Evidence Temperature-sensitive inactivation, proteomic analysis of pre-ribosomal particles, and Northern blot processing assays in S. cerevisiae

    PMID:15100437

    Open questions at the time
    • Whether Rrp1p has catalytic activity or is a scaffold unresolved
    • Direct RNA contacts not mapped
  11. 2011 Medium

    Provided a molecular mechanism for human RRP1 in pre-ribosome remodeling: competition with fibrillarin for p32 binding to drive particle splitting.

    Evidence Mass-spectrometry interactome, immunoblotting, cell fractionation, ultracentrifugation, and siRNA knockdown in human cells

    PMID:21536856

    Open questions at the time
    • Competitive exchange model inferred rather than directly visualized
    • Structural basis of the p32 interaction unknown
  12. 2015 High

    Defined the precise pre-rRNA cleavage step controlled by human RRP1, assigning it to ITS1 site 2 cleavage on the 90S particle and showing functional interplay with XRN2.

    Evidence Single and double siRNA knockdown with pre-rRNA processing analysis, fractionation, immunofluorescence, and actinomycin D treatment in human cells

    PMID:25969445

    Open questions at the time
    • Whether RRP1 itself cleaves or recruits a nuclease is unresolved
    • RNA-binding determinants on RRP1 not mapped
  13. 2013 Medium

    Established that the S. pombe protein named Rrp1 functions in homologous recombination, forming a complex with Rrp2 and Swi5 in an SDSA sub-pathway.

    Evidence Yeast two-hybrid, MMS-induced foci microscopy, and genetic epistasis with HR mutants in S. pombe

    PMID:23828040

    Open questions at the time
    • Biochemical activity not defined in this study
    • Direct DNA or Rad51 engagement not yet shown
  14. 2020 Medium

    Revealed that S. pombe Rrp1 modulates centromeric nucleosome dynamics, linking its translocase activity to chromosome stability and histone homeostasis.

    Evidence Overexpression, chromosome stability assays, histone immunoblotting, Cnp1 localization microscopy, and translocase-domain mutant analysis

    PMID:31932509

    Open questions at the time
    • Effect studied via overproduction rather than physiological levels
    • Direct nucleosome remodeling not reconstituted
  15. 2021 High

    Reconstituted the biochemical activities of S. pombe Rrp1 as a Rad51-stripping DNA translocase and Rad51-directed E3 ubiquitin ligase that restrains genome destabilization.

    Evidence Purified-protein DNA binding, ATPase, translocase, and ubiquitin ligase assays plus in vivo overexpression toxicity rescue and centromere ChIP in S. pombe

    PMID:34157114

    Open questions at the time
    • Relationship of these activities to the human/fly proteins of the same name unestablished
    • Endogenous regulation of the translocase/ligase switch unknown
  16. 2025 Medium

    Uncovered a non-ribosomal function for human RRP1 as an mRNA-binding suppressor of TYMS that dampens one-carbon-metabolism-driven inflammation in macrophages.

    Evidence Global RNA-protein interactome purification, RNA-binding validation, siRNA knockdown, and myeloid-specific knockout mouse arthritis model

    PMID:40715096

    Open questions at the time
    • Relationship between this cytoplasmic mRNA-regulatory role and the nucleolar rRNA-processing role unresolved
    • RNA-binding domain on RRP1 not mapped
  17. 2025 Medium

    Defined a neuronal redox function for Drosophila Rrp1 in long-term memory, mechanistically tying its APE1-like redox activity to Period and CaMKII expression.

    Evidence Neuron-specific RNAi and overexpression, E3330 pharmacological inhibition, aversive olfactory memory assays, and human APE1 transgenic rescue in Drosophila

    PMID:41289397

    Open questions at the time
    • Direct redox targets of Rrp1 in neurons not identified
    • Connection between DNA-repair and redox-signaling roles unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved whether the nucleolar rRNA-processing RRP1 and the cytoplasmic TYMS-mRNA-suppressing RRP1 are the same human protein operating in two compartments, and how the species-specific DNA-repair, HR-translocase, and ribosome-biogenesis activities relate at the gene level.
  • No study bridges the human nucleolar and macrophage functions
  • Orthology relationships among the species-specific activities are not experimentally established in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016787 hydrolase activity 4 GO:0003723 RNA binding 3 GO:0140097 catalytic activity, acting on DNA 3 GO:0003677 DNA binding 2 GO:0016874 ligase activity 1 GO:0140657 ATP-dependent activity 1
Localization
GO:0005634 nucleus 3 GO:0005730 nucleolus 3
Pathway
R-HSA-73894 DNA Repair 4 R-HSA-8953854 Metabolism of RNA 4 R-HSA-168256 Immune System 1
Partners
C1QBPFBLRAD51RRP2SWI5TYMSXRN2
Complex memberships
66S pre-ribosomal particle90S pre-ribosomal particle

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1991 Drosophila Rrp1 (recombination repair protein 1) possesses apurinic endonuclease activity, double-stranded DNA 3'-exonuclease activity, single-stranded DNA renaturation activity (Mg2+-dependent), and DNA strand transfer activity. The C-terminal 252-aa region (homologous to E. coli exonuclease III and S. pneumoniae exonuclease A) is responsible for the nuclease activities, while the unique N-terminal 427-aa region contributes to strand transfer and ssDNA renaturation. Protein purification from Drosophila embryo extracts; in vitro enzymatic assays; sequence homology analysis; column chromatography co-migration of activities Proceedings of the National Academy of Sciences of the United States of America High 1713691
1991 The C-terminal exonuclease domain of Drosophila Rrp1 is required for DNA strand transfer activity in vitro; a C-terminally deleted mutant lacking nuclease activity cannot perform strand transfer, but strand transfer can be restored by providing E. coli exonuclease III in trans, demonstrating that 3'-exonuclease activity is necessary for the strand transfer reaction. E. coli overexpression of Rrp1 and truncation mutant; in vitro DNA strand transfer assay; complementation with exogenous exonuclease III Nucleic acids research High 1653418 7678415
1993 Drosophila Rrp1 is a class II apurinic endonuclease that cleaves the phosphodiester backbone at one position 5' to the apurinic site, leaving a 3'-hydroxyl terminus that supports DNA synthesis. The specific activity is ~1×10^5 units/mg. Cleavage is specific to double-stranded DNA at the abasic site; the complementary strand and single-stranded substrates are not cleaved. In vitro endonuclease assay with 5'-end-labeled 37-bp oligonucleotide containing a single apurinic site; gel mobility analysis; DNA polymerase extension assay Biochemistry High 7692963
1993 Expression of Drosophila Rrp1 in repair-deficient E. coli (xth nfo double mutants) confers resistance to oxidative (H2O2, t-BuOOH, bleomycin) and alkylating (MMS, mitomycin C) agents. Complementation requires the C-terminal nuclease domain of Rrp1 but not the N-terminal domain, and is accompanied by up to 12-fold increase in AP endonuclease activity in cell extracts. Expression of Rrp1 constructs in repair-deficient E. coli strains BW528 and LG101; survival assays with DNA-damaging agents; AP endonuclease activity measurement in extracts Nucleic acids research High 7694234
1994 Site-directed mutagenesis of conserved residues in the Drosophila Rrp1 nuclease domain identified Glu-461 as essential for AP endonuclease activity; Lys-463 and Thr-462 influence substrate specificity of the nuclease. Mutants T462A, K463Q, and L484P retain protection against MMS but not against oxidative damage, demonstrating distinct specificity for alkylation versus oxidative substrates. Site-directed mutagenesis; E. coli complementation assays; purification and in vitro enzymatic activity measurements (AP endonuclease, 3'-phosphodiesterase) The Journal of biological chemistry High 7798276
1995 Drosophila Rrp1 possesses 3'-phosphodiesterase activity (removing 3'-phosphoglycolate termini generated by oxygen radical-induced DNA cleavage) and 3'-phosphatase activity. The 3'-phosphatase activity is at least 25-fold lower than phosphodiesterase or AP endonuclease activity. The phosphodiesterase releases a 3'-hydroxyl terminus. High NaCl reduces exonuclease 25-fold but does not inhibit phosphodiesterase. In vitro assays with site-specifically damaged oligonucleotide substrates (3'-phosphoglycolate from Fe(II)-bleomycin cleavage); gel mobility shift; DNA synthesis stimulation assay Biochemistry High 7530050
1996 Drosophila Rrp1 3'-exonuclease activity exhibits DNA sequence dependence and strand specificity: it is more efficient in purine-rich than pyrimidine-rich regions, with purine-purine and 3'-pyrimidine-5'-purine dinucleotide bonds cleaved faster than 3'-purine-5'-pyrimidine or pyrimidine-pyrimidine bonds. In vitro dsDNA 3'-exonuclease assays with defined oligonucleotide substrates of varying sequence composition; gel analysis Nucleic acids research Medium 8918793
1996 Overexpression of wild-type Drosophila Rrp1 from a heat-shock-inducible transgene reduces somatic mutation and recombination frequency induced by oxidative DNA-damaging agents (gamma-rays, bleomycin, paraquat) but not by alkylating agents (MMS, MNU), demonstrating a lesion-specific in vivo role in oxidative DNA damage repair. Drosophila w/w+ mosaic eye system (loss-of-heterozygosity assay); transgenic overexpression; heat-shock induction; treatment with multiple DNA-damaging agents Proceedings of the National Academy of Sciences of the United States of America High 8643678
1998 Drosophila Rrp1 has a bipartite domain structure: a highly organized, globular, predominantly alpha-helical C-terminal domain (Rrp1-C274, from Thr-406 onward) and an N-terminal ~399-aa region that is predominantly random coil and asymmetric. Both intact Rrp1 and Rrp1-C274 are monomers. The isolated C-terminal domain retains AP endonuclease activity at wild-type levels but has reduced 3'-exonuclease (210-fold) and 3'-phosphodiesterase (6.8-fold) activities. Limited proteolysis with endoproteinase Glu-C; biophysical analysis (circular dichroism, frictional coefficients); in vitro enzymatic assays of isolated domains The Journal of biological chemistry Medium 9852053
1987 The yeast (S. cerevisiae) RRP1 gene is required for processing of 27S pre-rRNA to mature 25S and 5.8S rRNAs. The rrp1 mutant also shows hypersensitivity to aminoglycoside antibiotics and a reduced 25S/18S rRNA ratio. Temperature-sensitive mutant analysis; RNA processing assays; genetic mapping; gene cloning Journal of bacteriology Medium 3549696
1990 In S. cerevisiae, suppressor gene SRD1 was identified by second-site suppressor screening of rrp1-1 mutants; loss-of-function srd1 alleles suppress the pre-rRNA processing defect, drug sensitivity, and thermolethality of the rrp1-1 point mutation but cannot suppress an rrp1 null allele, suggesting the SRD1 gene product interacts with or regulates the RRP1 product. Second-site suppressor screen; genetic analysis; allele-specific suppression test with disruption allele Genetics Medium 2179050
2004 S. cerevisiae Rrp1p is a nucleolar protein associated with several distinct 66S pre-ribosomal particles containing ribosomal proteins plus at least 28 nonribosomal proteins. Inactivation of Rrp1p blocks processing of 27SA3 to 27SBS pre-rRNA and of 27SB pre-rRNA to 7S plus 25.5S pre-rRNA, causing accumulation of 66S particles containing 27SA3 and 27SB(L) pre-rRNAs. Temperature-sensitive mutant inactivation; proteomic analysis of pre-ribosomal particles; RNA processing assays (Northern blot); subcellular localization (nucleolar) RNA (New York, N.Y.) High 15100437
1999 Human Nop52 (RRP1/NNP-1) is a nucleolar protein that localizes to the granular external domain of the nucleolus, excluded from rRNA transcription sites, and colocalizes with late rRNA-processing factors hPop1 and protein B23. During nucleologenesis at the end of mitosis, Nop52 is recruited at late stages via the prenucleolar body pathway, after fibrillarin and nucleolin. Immunocytochemistry with human autoantibodies; transfection of cDNA in mammalian cells; cell cycle analysis; colocalization studies with known nucleolar proteins Journal of cell science High 10341208
2011 Human p32 (splicing factor 2-associated protein) directly interacts with Nop52 (RRP1/NNP-1). Nop52 competes with fibrillarin (FBL) for binding to p32 in the nucleolus. Knockdown of p32 slows early rRNA processing (47S/45S to 18S and 32S pre-rRNA). p32 is present in pre-ribosomal fractions and associates with 47S/45S and 32S pre-rRNAs, suggesting that the competitive exchange of FBL for Nop52 on p32 drives remodeling from pre-90S to pre-40S and pre-60S particles. Mass spectrometry-based interactome; immunoblotting; immunocytochemistry; cell fractionation; ultracentrifugation; siRNA knockdown; co-localization analysis Molecular & cellular proteomics : MCP Medium 21536856
2015 Human RRP1 (Nop52/NNP-1) is required for site 2 cleavage in ITS1 of 47S/45S, 41S, and 36S pre-rRNAs. RRP1 knockdown suppresses site 2 cleavage, and double knockdown of XRN2 and RRP1 shows RRP1 accelerates this cleavage. RRP1 is present in the 90S pre-ribosomal particle and localizes to the dense fibrillar component of the nucleolus in an RNA Pol I transcription-dependent manner. siRNA knockdown (single and double with XRN2); pre-rRNA processing analysis; subcellular fractionation; immunofluorescence; actinomycin D treatment Nucleic acids research High 25969445
2021 S. pombe Rrp1 (ortholog of S. cerevisiae Uls1, a Rad5/16-like SWI2/SNF2 translocase) directly interacts with Rad51, removes Rad51 from double-stranded DNA in an ATPase-dependent manner, and possesses E3 ubiquitin ligase activity with Rad51 as a substrate. Rrp1 also binds DNA and has DNA-dependent ATPase activity. These activities restrict genome destabilization caused by excessive Rad51. Purified protein biochemistry (DNA binding, ATPase assay, translocase assay, ubiquitin ligase assay); pull-down/direct interaction; in vivo overexpression toxicity rescue; centromere ChIP Nucleic acids research High 34157114
2013 S. pombe Rrp1 and Rrp2 interact with each other and with Swi5 (HR mediator) via yeast two-hybrid. They form co-localizing MMS-induced nuclear foci, suggesting they function as a complex. Epistasis analysis places Rrp1 in the Srs2/Swi5-dependent synthesis-dependent strand annealing HR sub-pathway, independently of Rad57 and Rqh1. Yeast two-hybrid; microscopy (foci formation); genetic epistasis analysis with HR mutants; recombination frequency measurements Nucleic acids research Medium 23828040
2020 S. pombe Rrp1 overproduction leads to chromosome instability, growth defects, reduction in global histone levels, and mislocalization of centromere-specific histone Cnp1, phenotypes that depend on the putative DNA translocase activity of Rrp1, indicating Rrp1 modulates nucleosome dynamics at centromeres. Overexpression studies; chromosome stability assays; histone level analysis (immunoblot); Cnp1 localization by microscopy; domain mutant analysis Journal of cell science Medium 31932509
2025 Human RRP1 acts as an RNA-binding protein that binds nuclear TYMS (thymidylate synthase) transcript and suppresses TYMS expression post-transcriptionally in inflammatory macrophages, thereby reducing folate/one-carbon metabolism and dampening innate inflammatory responses. Myeloid-specific RRP1-deficient mice develop severe experimental arthritis with increased pro-inflammatory cytokines. Global RNA-protein interactome purification (GRPIp); RNA-binding validation; siRNA knockdown; myeloid-specific knockout mouse model (experimental arthritis); cytokine measurement; TYMS expression analysis Nature communications Medium 40715096
2025 In Drosophila, Rrp1 (APE1 homolog) acts as a redox regulator of long-term memory (LTM) in dorsal-anterior-lateral neurons. Rrp1 knockdown impairs LTM formation; overexpression enhances retention. Pharmacological inhibition of Rrp1 redox activity (E3330) suppresses Period and CaMKII expression. Human APE1 redox activity rescues memory deficits in Rrp1-deficient flies and promotes Period synthesis. Rrp1 is required for CREBA-mediated LTM acceleration. Neuron-specific RNAi knockdown; overexpression; pharmacological inhibition with E3330; behavioral assays (aversive olfactory LTM); transgenic rescue with human APE1; gene expression analysis Proceedings of the National Academy of Sciences of the United States of America Medium 41289397

Source papers

Stage 0 corpus · 32 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 Rrp1, a cyclic-di-GMP-producing response regulator, is an important regulator of Borrelia burgdorferi core cellular functions. Molecular microbiology 113 19210621
2004 Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation. RNA (New York, N.Y.) 85 15100437
2011 The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes. Molecular microbiology 82 21542866
1991 Drosophila Rrp1 protein: an apurinic endonuclease with homologous recombination activities. Proceedings of the National Academy of Sciences of the United States of America 72 1713691
1999 The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis. Journal of cell science 65 10341208
2013 Study of the response regulator Rrp1 reveals its regulatory role in chitobiose utilization and virulence of Borrelia burgdorferi. Infection and immunity 61 23478317
1987 RRP1, a Saccharomyces cerevisiae gene affecting rRNA processing and production of mature ribosomal subunits. Journal of bacteriology 43 3549696
1991 Cloning and characterization of Rrp1, the gene encoding Drosophila strand transferase: carboxy-terminal homology to DNA repair endo/exonucleases. Nucleic acids research 42 1653418
2011 Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles. Molecular & cellular proteomics : MCP 33 21536856
1995 Characterization of the nuclease activity of Drosophila Rrp1 on phosphoglycolate- and phosphate-modified DNA 3'-termini. Biochemistry 23 7530050
1993 Drosophila Rrp1 complements E. coli xth nfo mutants: protection against both oxidative and alkylation-induced DNA damage. Nucleic acids research 23 7694234
1993 Expression of Drosophila Rrp1 protein in Escherichia coli. Enzymatic and physical characterization of the intact protein and a carboxyl-terminally deleted exonuclease-deficient mutant. The Journal of biological chemistry 21 7678415
2015 Human nucleolar protein Nop52 (RRP1/NNP-1) is involved in site 2 cleavage in internal transcribed spacer 1 of pre-rRNAs at early stages of ribosome biogenesis. Nucleic acids research 18 25969445
1994 Single amino acid changes alter the repair specificity of Drosophila Rrp1. Isolation of mutants deficient in repair of oxidative DNA damage. The Journal of biological chemistry 18 7798276
2004 Upregulation of the NNP-1 (novel nuclear protein-1, D21S2056E) gene in keloid tissue determined by cDNA microarray and in situ hybridization. The British journal of dermatology 16 15606508
1996 Drosophila Rrp1 3'-exonuclease: demonstration of DNA sequence dependence and DNA strand specificity. Nucleic acids research 16 8918793
1996 Overexpression of a Rrp1 transgene reduces the somatic mutation and recombination frequency induced by oxidative DNA damage in Drosophila melanogaster. Proceedings of the National Academy of Sciences of the United States of America 15 8643678
2009 The role of novel genes rrp1(+) and rrp2(+) in the repair of DNA damage in Schizosaccharomyces pombe. DNA repair 13 19185548
2002 Novel products of the HUD, HUC, NNP-1 and alpha-internexin genes identified by autologous antibody screening of a pediatric neuroblastoma library. International journal of cancer 13 12209604
1993 Characterization of the apurinic endonuclease activity of Drosophila Rrp1. Biochemistry 13 7692963
1990 srd1, a Saccharomyces cerevisiae suppressor of the temperature-sensitive pre-rRNA processing defect of rrp1-1. Genetics 13 2179050
1997 The NNP-1 gene (D21S2056E), which encodes a novel nuclear protein, maps in close proximity to the cystatin B gene within the EPM1 and APECED critical region on 21q22.3. Genomics 11 9192856
2021 Rrp1 translocase and ubiquitin ligase activities restrict the genome destabilising effects of Rad51 in fission yeast. Nucleic acids research 8 34157114
2013 Involvement of Schizosaccharomyces pombe rrp1+ and rrp2+ in the Srs2- and Swi5/Sfr1-dependent pathway in response to DNA damage and replication inhibition. Nucleic acids research 8 23828040
1998 Drosophila Rrp1 domain structure as defined by limited proteolysis and biophysical analyses. The Journal of biological chemistry 8 9852053
2024 MCP5, a methyl-accepting chemotaxis protein regulated by both the Hk1-Rrp1 and Rrp2-RpoN-RpoS pathways, is required for the immune evasion of Borrelia burgdorferi. PLoS pathogens 6 39775665
2025 The RNA-binding protein RRP1 brakes macrophage one-carbon metabolism to suppress autoinflammation. Nature communications 5 40715096
2022 Rrp1, Rrp2 and Uls1 - Yeast SWI2/SNF2 DNA dependent translocases in genome stability maintenance. DNA repair 5 35716431
2024 MCP5, a methyl-accepting chemotaxis protein regulated by both the Hk1-Rrp1 and Rrp2-RpoN-RpoS pathways, is required for the immune evasion of Borrelia burgdorferi. bioRxiv : the preprint server for biology 2 38915556
2020 Schizosaccharomyces pombe DNA translocases Rrp1 and Rrp2 have distinct roles at centromeres and telomeres that ensure genome stability. Journal of cell science 2 31932509
2025 Redox regulation of memory formation by Rrp1 in Drosophila. Proceedings of the National Academy of Sciences of the United States of America 1 41289397
2024 Replication stress response in fission yeast differentially depends on maintaining proper levels of Srs2 helicase and Rrp1, Rrp2 DNA translocases. PloS one 1 38905307

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