ArticleThe EMBO journal2005
The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Unwinding the Role of the CMG Helicase in Inborn Errors of Immunity.Journal of clinical immunology · 2023Article
- Possible Contribution of Alternative Transcript Isoforms in Mature Biofilm Growth Phase ofIndian journal of microbiology · 2022Article
- Inhibition of DNA replication initiation by silver nanoclusters.Nucleic acids research · 2021Article
- The Human Replicative Helicase, the CMG Complex, as a Target for Anti-cancer Therapy.Frontiers in molecular biosciences · 2018Review
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- Origin licensing requires ATP binding and hydrolysis by the MCM replicative helicase.Molecular cell · 2014Article
- Multiple functions for Mcm2-7 ATPase motifs during replication initiation.Molecular cell · 2014Article
- The ORC/Cdc6/MCM2-7 complex facilitates MCM2-7 dimerization during prereplicative complex formation.Nucleic acids research · 2014Article
- Prereplication-complex formation: a molecular double take?Nature structural & molecular biology · 2014Article
- Helicase loading at chromosomal origins of replication.Cold Spring Harbor perspectives in biology · 2013Review
- In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2-7 hexamer dimerization.Nucleic acids research · 2013Article
- Depletion of cellular pre-replication complex factors results in increased human cytomegalovirus DNA replication.PloS one · 2012Article
- Multiple Cdt1 molecules act at each origin to load replication-competent Mcm2-7 helicases.The EMBO journal · 2011Article
- Article
- Pre-replication complex proteins assemble at regions of low nucleosome occupancy within the Chinese hamster dihydrofolate reductase initiation zone.Nucleic acids research · 2011Article
- C. elegans MCM-4 is a general DNA replication and checkpoint component with an epidermis-specific requirement for growth and viability.Developmental biology · 2011Article
- A human B-cell interactome identifies MYB and FOXM1 as master regulators of proliferation in germinal centers.Molecular systems biology · 2010Article
- Origin-dependent initiation of DNA replication within telomeric sequences.Nucleic acids research · 2010Article
- Mathematical modelling of eukaryotic DNA replication.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2010Article
- The Mcm complex: unwinding the mechanism of a replicative helicase.Microbiology and molecular biology reviews : MMBR · 2009Review
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2 authors.
Funding
Abstract
Eukaryotes have six minichromosome maintenance (MCM) proteins that are essential for DNA replication. The contribution of ATPase activity of MCM complexes to their function in replication is poorly understood. We have established a cell-free system competent for replication in which all MCM proteins are supplied by purified recombinant Xenopus MCM complexes. Recombinant MCM2-7 complex was able to assemble onto chromatin, load Cdc45 onto chromatin, and restore DNA replication in MCM-depleted extracts. Using mutational analysis in the Walker A motif of MCM6 and MCM7 of MCM2-7, we show that ATP binding and/or hydrolysis by MCM proteins is dispensable for chromatin loading and pre-replicative complex (pre-RC) assembly, but is required for origin unwinding during DNA replication. Moreover, this ATPase-deficient mutant complex did not support DNA replication in MCM-depleted extracts. Altogether, these results both demonstrate the ability of recombinant MCM proteins to perform all replication roles of MCM complexes, and further support the model that MCM2-7 is the replicative helicase. These data establish that mutations affecting the ATPase activity of the MCM complex uncouple its role in pre-RC assembly from DNA replication.
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