| 1991 |
MCM2 and MCM3 encode structurally related proteins essential for ARS-specific minichromosome maintenance and initiation of DNA replication in S. cerevisiae; MCM2 contains a putative zinc-finger domain essential for function, and genetic studies show MCM2 and MCM3 play interacting roles in DNA replication. |
Genetic analysis, double-mutant lethality, overexpression suppression, sequence analysis |
Genes & development |
High |
2044961
|
| 1993 |
Fission yeast nda1+ and nda4+, orthologues of budding yeast MCM2 and CDC46, are essential for S-phase initiation; mutations cause a reversible cell cycle block at the onset of DNA synthesis. |
Complementation cloning, temperature-sensitive mutant analysis, DNA content analysis, gene disruption |
Molecular biology of the cell |
High |
8298187
|
| 1995 |
Human BM28 (MCM2) is chromatin-associated in G1/early S phase (DNase I-sensitive), is progressively lost from chromatin as S phase proceeds, and undergoes cell-cycle-regulated changes in electrophoretic mobility consistent with phosphorylation; hyperphosphorylation of the fast-migrating form correlates with chromatin dissociation. |
Triton X-100 extraction, DNase I digestion, cell cycle fractionation, immunoblotting |
The Journal of cell biology |
High |
7790346
|
| 1997 |
Cdc7-Dbf4 kinase physically interacts with Mcm2 and phosphorylates Mcm2 (and other MCM2-7 members) in vitro; a dbf4 suppressor mutation restores DNA synthesis initiation to mcm2-1 mutants, placing Cdc7-Dbf4 phosphorylation of Mcm2 as a critical step at the G1-to-S transition. |
Suppressor screen, in vitro kinase assay, genetic epistasis, physical interaction assay |
Genes & development |
High |
9407029
|
| 2000 |
MCM complexes are required not only for initiation but also for elongation of DNA replication forks in S. cerevisiae; depletion of MCMs after initiation irreversibly blocks replication fork progression. |
Conditional degron mutants, BrdU incorporation, DNA fiber analysis |
Science (New York, N.Y.) |
High |
10834843
|
| 2001 |
Mouse Mcm2 inhibits the DNA helicase activity of the Mcm4,6,7 complex; the C-terminal half of Mcm2 binds Mcm4 to disassemble the Mcm4,6,7 hexamer; the N-terminal region contains major Cdc7-mediated phosphorylation sites; and Mcm2 can assemble a nucleosome-like structure in vitro with H3/H4 histones, with the N-terminal region required for histone binding. |
In vitro helicase inhibition assay, deletion mutagenesis, in vitro kinase assay, nucleosome assembly assay |
The Journal of biological chemistry |
High |
11568184
|
| 2001 |
MCM2 interacts directly with the histone acetyltransferase HBO1 (a MYST family member); an N-terminal domain of MCM2 is required for HBO1 binding; the C2HC zinc finger of HBO1 mediates the interaction; reverse yeast two-hybrid and suppressor analysis confirm direct interaction. |
Yeast two-hybrid, in vitro binding, co-immunoprecipitation, reverse two-hybrid, suppressor mutagenesis |
The Journal of biological chemistry |
High |
11278932
|
| 2002 |
Budding yeast Cdt1 interacts with the Mcm2-7 complex, and nuclear accumulation of Cdt1 and Mcm2-7 during G1 is interdependent; CDKs exclude both Cdt1 and Mcm2-7 from the nucleus later in the cell cycle. |
Co-immunoprecipitation, cell cycle fractionation, genetic interaction |
Nature cell biology |
High |
11836525
|
| 2002 |
In Xenopus, Mcm10 binds chromatin downstream of Mcm2-7 pre-RC assembly (requires chromatin-bound Mcm2-7) and is required for subsequent Cdc45 loading, RPA binding, and origin unwinding. |
Xenopus egg extract depletion/add-back, chromatin binding assays |
Molecular cell |
High |
11864598
|
| 2004 |
ORC ATP hydrolysis (requiring Orc1 and Orc4 subunits) drives reiterative loading of multiple Mcm2-7 complexes at origins; blocking ORC ATPase prevents repeated Mcm2-7 loading. |
In vitro reconstitution of pre-RC, ATPase-deficient ORC mutants, biochemical loading assays |
Molecular cell |
High |
15610739
|
| 2005 |
The ATPase activity of MCM2-7 (specifically Walker A motif mutations in MCM6 and MCM7) is dispensable for chromatin loading and pre-RC assembly but is essential for origin DNA unwinding during replication. |
Reconstituted Xenopus MCM2-7 from purified recombinant proteins, Walker A mutagenesis, chromatin loading assay, DNA replication assay in MCM-depleted extracts |
The EMBO journal |
High |
16369567
|
| 2006 |
Cdc7 phosphorylates human MCM2 at multiple N-terminal sites (at least three Cdc7 sites, plus Cdk2/Cdk1 S/P sites and a CK2 site); Cdc7-phosphorylated MCM2 isoforms are predominantly not stably associated with chromatin; all sites identified in vitro are phosphorylated in cells. |
In vitro kinase assay, mass spectrometry, phospho-specific antibodies, cell cycle immunoblotting |
The Journal of biological chemistry |
High |
16446360
|
| 2006 |
Cdc7/Dbf4 phosphorylation of human MCM2 is essential for initiation of DNA replication in mammalian cells; phosphomimetic MCM2 (MCM2E) increases ATPase activity of the MCM2-7 complex and rescues replication after MCM2 siRNA knockdown, whereas non-phosphorylatable MCM2 (MCM2A) cannot. |
siRNA knockdown, phosphomimetic/non-phosphorylatable mutants, in vitro ATPase assay, immunofluorescence, automated cell imaging |
Molecular biology of the cell |
High |
16899510
|
| 2006 |
The Cdc45/Mcm2-7/GINS (CMG) complex was isolated from Drosophila embryo extracts as a stable, high-molecular-weight complex with associated ATP-dependent DNA helicase activity; RNAi of GINS and Cdc45 blocks S-phase transition. |
Immunoaffinity chromatography, helicase assay, RNAi knockdown |
Proceedings of the National Academy of Sciences of the United States of America |
High |
16798881
|
| 2007 |
Excess chromatin-bound Mcm2-7 licenses dormant replication origins in human cells that are normally suppressed by checkpoint activity; RNAi reduction of Mcm2-7 suppresses dormant origin use and sensitizes cells to replication inhibitors without affecting normal replication rates. |
RNAi knockdown, DNA fiber analysis, BrdU incorporation, replication inhibitor challenge |
Genes & development |
High |
18079179
|
| 2007 |
Orc6 is required for dynamic recruitment of Cdt1 during repeated Mcm2-7 loading; two regions of Orc6 bind Cdt1 directly; an ORC lacking Orc6 fails to load Mcm2-7; a Cdt1-Orc6-CTD fusion restores single-round but not multiple-round Mcm2-7 loading. |
In vitro reconstitution, direct binding assays, Orc6 depletion, fusion protein complementation |
Genes & development |
High |
18006685
|
| 2009 |
Mcm2-7 is loaded as a head-to-head double hexamer around double-stranded DNA during pre-RC formation; single heptamers of Cdt1•Mcm2-7 are cooperatively loaded; once loaded, Mcm2-7 double hexamers can slide passively along dsDNA. |
In vitro reconstitution with purified yeast proteins, electron microscopy, biochemical DNA-binding assays |
Cell |
High |
19896182
|
| 2009 |
MCM2-7 forms a double hexamer during pre-RC formation in vitro; before loading it is a single hexamer in solution; loaded MCM2-7 encircles DNA and can slide non-directionally; loading requires ORC, Cdc6, Cdt1, origin DNA, and ATP hydrolysis. |
In vitro reconstitution, electron microscopy, biochemical loading assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
19910535
|
| 2009 |
Assembly of the human CMG complex (Cdc45-Mcm2-7-GINS) occurs only after G1/S and requires CDK and Cdc7 kinase activity, as well as RecQL4, Ctf4/And-1, and Mcm10 proteins; TopBP1 is not required for CMG formation in human cells. |
Bimolecular fluorescence complementation (BiFC) in HeLa cells, siRNA depletion, CDK inhibitor treatment |
Proceedings of the National Academy of Sciences of the United States of America |
High |
19805216
|
| 2009 |
Incorporation of Mcm2-7 into the pre-RC changes the level and specificity of DDK (Cdc7-Dbf4) phosphorylation; DDK preferentially targets a conformationally distinct, tightly origin-DNA-linked subpopulation of Mcm2-7; DDK association requires prior phosphorylation of the pre-RC. |
In vitro kinase assay with pre-RC, origin DNA-binding assays, biochemical fractionation |
Genes & development |
High |
19270162
|
| 2009 |
MCM10 is essential for the integrity of the RECQ4-MCM replicative helicase complex; MCM10 interacts directly with RECQ4 and regulates its DNA unwinding activity; the RECQ4 chromatin complex contains MCM10, MCM2-7, CDC45, and GINS. |
Chromatin immunoprecipitation, co-immunoprecipitation, direct binding assay, helicase assay |
The EMBO journal |
High |
19696745
|
| 2009 |
Cyclin E-Cdk2 promotes Mcm2 loading onto chromatin in part by driving Cdc7 accumulation; phosphorylation of Mcm2 by Cdc7 is required for Mcm2 chromatin loading during cell cycle re-entry from quiescence; a phosphomimetic Mcm2 mutant bypasses the Cdc7 requirement for loading. |
Chromatin fractionation, immunoblotting, dominant-negative Cdk2 expression, phosphomimetic/non-phosphorylatable mutants |
Molecular cell |
High |
19647517
|
| 2009 |
In budding yeast, Dbf4 recruits Cdc7 to Mcm2 (Dbf4 alone binds Mcm2 tightly; Cdc7 alone binds weakly); DDK phosphorylates Mcm2 at Ser-164 and Ser-170; phosphorylation of Ser-170 is essential for cell growth and is bypassed by the mcm5-bob1 mutation. |
In vitro binding assay, in vitro kinase assay, yeast genetics, phosphosite mutagenesis |
The Journal of biological chemistry |
High |
19692334
|
| 2010 |
Drosophila MCM2-7 helicase is activated in the CMG complex with Cdc45 and GINS; CMG formation elevates ATP hydrolysis rates by ~100-fold, enables helicase activity on circular templates, and improves DNA substrate affinity; GINS binds specifically to MCM4. |
Recombinant protein reconstitution, ATPase assay, helicase assay, pairwise binding assays |
Molecular cell |
High |
20122406
|
| 2010 |
Mec1 (ATR orthologue) and other kinases prime Mcm2-7 by phosphorylating S/T-Q and S/T-P motifs on Mcm4 and Mcm6; this priming phosphorylation is required for subsequent DDK phosphorylation of Mcm2-7 and for normal S-phase; Mrc1 facilitates Mec1-dependent priming on chromatin-bound Mcm2-7. |
Phosphomimetic mutations, genetic epistasis, in vitro kinase assay, S-phase progression analysis |
Molecular cell |
High |
21070963
|
| 2010 |
MCM-BP can disassemble the MCM2-7 complex and functions as an unloader of MCM2-7 from chromatin at the end of S phase; MCM-BP accumulates in nuclei in late S phase, and its immunodepletion inhibits replication-dependent MCM dissociation without affecting pre-RC formation or DNA replication. |
Xenopus egg extract depletion, immunopurification, chromatin fractionation, recombinant protein assay |
Genes & development |
High |
21196493
|
| 2011 |
Electron microscopy of Mcm2-7 reveals two conformations: a lock-washer spiral and a planar gapped ring, with Mcm2 and Mcm5 flanking a breach; GINS and Cdc45 bridge this gap in the CMG complex to form a topologically closed assembly with a large interior channel; nucleotide binding further seals the Mcm2-Mcm5 discontinuity. |
Single-particle electron microscopy of Mcm2-7 and CMG complex |
Nature structural & molecular biology |
High |
21378962
|
| 2011 |
Human Ctf4 interacts with multiple components of the CMG complex; the hCtf4-CMG complex contains a homodimeric Ctf4 and monomeric CMG; homodimeric Ctf4 acts as a platform linking polymerase α to the CMG complex; the hCtf4-CMG complex has more salt-resistant helicase activity than CMG alone. |
In vitro interaction of purified proteins, co-infection in insect cells, HeLa chromatin immunoprecipitation, helicase assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
24255107
|
| 2011 |
Charge complementarity between Cdt1 and Mcm6 C-terminal domains mediates Cdt1-MCM2-7 interaction; NMR structure of the Cdt1(410-440)/MCM6(708-821) complex reveals the binding interface; alanine substitutions at conserved interacting residues in yeast are defective in DNA replication and Mcm2 chromatin loading. |
NMR structure determination, site-directed mutagenesis, yeast genetics, chromatin loading assay |
Nucleic acids research |
High |
22140117
|
| 2011 |
GINS and Sld3 compete for binding to Mcm2-7 and Cdc45; Sld3 forms a ternary CMS complex (Cdc45-Mcm2-7-Sld3), and GINS displaces Sld3 to form the CMG complex, consistent with a model in which GINS trades places with Sld3 to activate the replication fork helicase. |
In vitro binding assays, size exclusion chromatography, competition assays with purified proteins |
The Journal of biological chemistry |
High |
21362622
|
| 2012 |
TIM and TIPIN (replication fork regulators) interact predominantly with MCM3-7 subunits; the Rb N-terminal fragment binds MCM3, MCM6, and MCM7; these interactions were determined by co-immunoprecipitation from co-expressed insect cells. |
Co-immunoprecipitation from co-expressed Sf9 insect cells |
Journal of biochemistry |
Medium |
20299328
|
| 2012 |
The Mcm4(Chaos3) allele disrupts MCM4:MCM6 interaction and triggers miR-34-mediated downregulation of MCM2-7 mRNAs via a Dicer1/Drosha-dependent pathway; MCM3 also acts as a negative regulator of MCM2-7 in vivo by complexing with MCM5 via a nuclear-export-signal-like domain, blocking chromatin recruitment. |
Mouse genetics, microRNA profiling, co-immunoprecipitation, chromatin fractionation |
Nucleic acids research |
High |
22362746
|
| 2013 |
CDK2/cyclinA phosphorylation of MCM4 inhibits the DNA-binding ability of the MCM2-7 complex; changing six Ser/Thr residues in the MCM4 N-terminus to alanine renders MCM2-7 insensitive to CDK-mediated inhibition of DNA binding. |
In vitro phosphorylation, gel-shift DNA-binding assay, mutagenesis |
Journal of biochemistry |
High |
23864661
|
| 2013 |
An ORC/Cdc6/MCM2-7 (OCM) intermediate forms after Cdt1 release and ATP hydrolysis; OCM (not the initial OCCM) is competent for MCM2-7 dimerization and double-hexamer assembly; Orc1 and Cdc6 ATPase activities both promote OCM formation; CDK phosphorylation of ORC inhibits OCM formation to enforce once-per-cell-cycle replication. |
In vitro reconstitution, mutant analysis of ATP hydrolysis, biochemical complex isolation |
Molecular cell |
High |
23603117
|
| 2013 |
The ORC/Cdc6/MCM2-7 (OCM) complex facilitates MCM2-7 dimerization; MCM2-7 hexamer-interface mutants arrest after OCM formation but before double-hexamer assembly, identifying MCM2-7 dimerization as a distinct and limiting step in pre-RC assembly. |
In vitro reconstitution, hexamer-interface mutagenesis, biochemical complex analysis, yeast genetics |
Nucleic acids research |
High |
24234446
|
| 2013 |
Ciprofloxacin preferentially inhibits the DNA helicase activity of Mcm2-7 at concentrations that have little effect on other helicases; an mcm4(chaos3) mutation confers increased ciprofloxacin resistance, directly linking the drug target to Mcm2-7. |
In vitro helicase assay, yeast and human cell proliferation assay, structural analogue screen |
Bioscience reports |
High |
24001138
|
| 2014 |
Mcm2-7 ATPase motif mutations show that ATP binding and hydrolysis are required for helicase loading, with specific ATPase sites required for initial Mcm2-7 recruitment or Cdt1 release; a subset of ATPase mutants complete loading but cannot initiate replication, failing in DNA association maintenance, GINS recruitment, or DNA unwinding. |
Walker A/B mutagenesis of all six Mcm subunits, in vitro helicase loading assay, DNA unwinding assay |
Molecular cell |
High |
25087876
|
| 2014 |
ORC-Cdc6 loads single Cdt1-Mcm2-7 heptamers, then Cdt1 release and ORC-Cdc6-Mcm2-7 complex formation precede recruitment of a second Mcm2-7 hexamer; structural EM evidence for ORC-Cdc6-Mcm2-7 and ORC-Cdc6-Mcm2-7-Mcm2-7 intermediates; the loaded double hexamer head-to-head interface creates a binding site for S-phase kinase. |
Electron microscopy, in vitro reconstitution, biochemical intermediate analysis |
Genes & development |
High |
25319829
|
| 2014 |
The Mcm2-Mcm5 interface serves as the unique DNA entry gate during regulated helicase loading; chemical crosslinking of this gate blocks ORC-Cdc6-Cdt1-dependent loading and triggers ATPase-driven complex disassembly in vitro; Mcm2/Mcm5 gate opening is essential for chromatin loading and cell cycle progression in vivo. |
Chemical biology (crosslinking), in vitro loading assay, ATPase assay, yeast genetics |
Genes & development |
High |
25085418
|
| 2015 |
Human MCM2 chaperones histones H3-H4 via its histone-binding domain (HBD); crystal structure shows an H3-H4 tetramer bound by two MCM2 HBDs hijacking nucleosomal DNA-binding sites; a second structure shows MCM2 and ASF1 co-chaperoning an H3-H4 dimer; MCM2 HBD mutation impairs MCM2-7 histone-chaperone function and normal cell proliferation. |
Crystal structure determination, mutational analysis, cell proliferation assay |
Nature structural & molecular biology |
High |
26167883
|
| 2015 |
DNA translocases including RNA polymerase can push Mcm2-7 double hexamers along DNA after loading; displaced Mcm2-7 can still support DNA replication initiation distal to the loading site; in yeast defective for transcription termination, RNA polymerase collisions redistribute Mcm2-7 and shift replication initiation sites. |
In vitro translocase-Mcm2-7 interaction assay, DNA replication assay, genome-wide Mcm2-7 mapping, yeast genetics |
Molecular cell |
High |
26656162
|
| 2015 |
PTEN physically associates with MCM2, dephosphorylates MCM2 at Ser-41, and restricts replication fork progression under replicative stress; PTEN disruption results in unrestrained fork progression similar to the phosphomimetic MCM2-S41D mutant; PTEN is required for prevention of chromosomal aberrations under replication stress. |
Co-immunoprecipitation, phosphatase assay, DNA fiber analysis, phosphomimetic mutants, chromosomal aberration assay |
Cell reports |
High |
26549452
|
| 2017 |
Cryo-EM structure of the OCCM (ORC-Cdc6-Cdt1-Mcm2-7) at 3.9 Å shows flexible Mcm2-7 winged-helix domains engaging ORC-Cdc6; Cdt1 embraces Mcm2, Mcm4, and Mcm6 with a three-domain configuration; DNA passes through both rings; Orc4 α-helix and positively charged loops of Orc2/Cdc6 contact origin DNA; the Mcm2-7 C-tier ring is topologically closed by an Mcm5 loop around Mcm2 while the N-tier Mcm2-Mcm5 interface remains open. |
Cryo-EM structure determination at 3.9 Å |
Nature structural & molecular biology |
High |
28191893
|
| 2017 |
Cryo-EM of Mcm2-7 double hexamer on dsDNA shows DNA is zigzagged inside the central channel; PS1 loops of Mcm3, 4, 6, 7 (but not 2 and 5) engage the lagging strand with ~1 base per subunit step size; the staggered hexamers position each DNA strand against the Mcm2-Mcm5 gates, suggesting lagging-strand extrusion initiates at the zinc-finger domain interface. |
Cryo-EM structure of Mcm2-7 double hexamer on dsDNA |
Proceedings of the National Academy of Sciences of the United States of America |
High |
29078375
|
| 2017 |
The yeast MCM hexamer and Cdt1-MCM heptamer adopt left-handed coil structures with a 10-15 Å gap between Mcm5 and Mcm2; Cdt1 wraps around the N-terminal regions of Mcm2, Mcm6, and Mcm4; the Mcm5 WHD occludes the central channel; these open-ring precursor structures suggest a spring-action model for helicase loading and origin melting. |
Cryo-EM structure determination of yeast MCM hexamer and Cdt1-MCM heptamer |
Nature structural & molecular biology |
High |
28191894
|
| 2017 |
Single-molecule FRET and colocalization spectroscopy show that Mcm2-7 rings are open during initial DNA association and close sequentially (concomitant with Cdt1 release); Mcm2-7 ATP hydrolysis is coupled to ring closure and Cdt1 release; the first Mcm2-7 must load before the second can be recruited. |
Single-molecule FRET, colocalization single-molecule spectroscopy (CoSMoS) |
Nature structural & molecular biology |
High |
28191892
|
| 2018 |
MCM2, as part of the replicative helicase, ensures symmetric inheritance of parental histone H3-H4 to both sister chromatids; histone-binding mutations in MCM2 increase leading-strand bias of parental histone segregation and exacerbate histone PTM asymmetry between sister chromatids. |
SCAR-seq (sister chromatid analysis of replication), histone PTM partition measurement in embryonic stem cells |
Science (New York, N.Y.) |
High |
30115746
|
| 2018 |
O-GlcNAc transferase (OGT) stably interacts with multiple MCM2-7 subunits; all six MCM2-7 subunits are O-GlcNAcylated predominantly in the chromatin-bound fraction; OGT silencing decreases chromatin binding of MCM2, MCM6, and MCM7, and destabilizes MCM2/6 and MCM4/7 interactions in chromatin. |
Co-immunoprecipitation, mass spectrometry, siRNA silencing, chromatin fractionation |
Cellular and molecular life sciences : CMLS |
Medium |
30069701
|
| 2019 |
A conserved Mcm4 motif is required for stable MCM2-7 double-hexamer formation; mutations permitting loading of two Mcm2-7 complexes but blocking double-hexamer stability demonstrate that double-hexamer formation is required for extensive origin DNA unwinding but not initial DNA melting or recruitment of Cdc45, GINS, or Mcm10. |
Single-molecule assays, biochemical reconstitution, kinetic analysis |
eLife |
High |
31385807
|
| 2019 |
MCM2 has a non-replicative role in ciliogenesis in non-cycling human fibroblasts and zebrafish; MCM2 binds to transcription start sites of cilia-inhibiting genes in post-mitotic cells, and its loss promotes transcription of these genes, causing cilia shortening and centriole overduplication. |
ChIP, siRNA knockdown in non-cycling fibroblasts, zebrafish morpholino depletion, cilia length measurement |
Nucleic acids research |
Medium |
30329080
|
| 2021 |
DDK phosphorylation of multiple sites on Mcm2-7 N-terminal tails modulates the number of Cdc45-tail-GINS (CtG) intermediates formed per Mcm2-7 in a first recruitment stage; higher CtG multiplicity increases the frequency of CMG formation in a second, inefficient conversion step. |
Single-molecule biochemical assays for CMG formation, phosphorylation site mutagenesis |
eLife |
High |
33616038
|
| 2022 |
Cryo-EM and biochemical analysis shows that the Dbf4 HBRCT domain anchors DDK to Mcm2 as a docking point; this supports DDK binding across the MCM2-7 double-hexamer interface, allowing phosphorylation of Mcm4 on the opposite hexamer; DDK rotation around the Mcm2 anchor allows phosphorylation of Mcm2 and Mcm6. |
Cryo-EM, biochemical analysis, DDK-MCM2-7 interaction mapping |
Nature communications |
High |
35614055
|
| 2022 |
MCMBP associates with MCM3 and is required for assembly of the MCM2-7 hexamer in human cells using nascent MCM3; acute MCMBP depletion reduces replication licensing; p53-null cells depleted of MCMBP enter S phase and accumulate DNA damage, while p53-positive cells arrest in G1. |
Auxin-inducible degron (AID) acute depletion, co-immunoprecipitation, flow cytometry, DNA damage markers |
eLife |
High |
35438632
|
| 2022 |
Mcm2 histone-binding function is required for silencing of pluripotent genes and induction of lineage-specific genes during embryonic stem cell differentiation; Mcm2-2A mutation (defective in histone binding) reduces binding of Asf1a (a histone chaperone that partners with Mcm2 for nucleosome disassembly at bivalent chromatin), reduces Mcm2 binding at gene promoters including bivalent domains, and decreases chromatin accessibility at these sites in neural precursor cells. |
ChIP-seq, ATAC-seq, co-immunoprecipitation, mouse ES cell differentiation assays |
eLife |
High |
36354740
|
| 2023 |
The N-terminus of Spt16 (FACT subunit) directly interacts with the replicative helicase MCM2-7 and facilitates formation of a ternary complex involving FACT, histone H3/H4, and the Mcm2 histone-binding domain; this interaction is required for efficient parental histone recycling and transfer to lagging strands during replication. |
Co-immunoprecipitation, ChIP-seq for histone partitioning, mutagenesis, FACT-MCM interaction assays in budding yeast |
Nucleic acids research |
High |
37850662
|