ArticleThe Journal of biological chemistry2008
Mcm subunits can assemble into two different active unwinding complexes.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Review
- Review
- Revealing the potential pathogenesis of glioma by utilizing a glioma associated protein-protein interaction network.Pathology oncology research : POR · 2015Article
- Juvenile hormone-receptor complex acts on mcm4 and mcm7 to promote polyploidy and vitellogenesis in the migratory locust.PLoS genetics · 2014Article
- The Mcm2-7 replicative helicase: a promising chemotherapeutic target.BioMed research international · 2014Review
- The fission yeast minichromosome maintenance (MCM)-binding protein (MCM-BP), Mcb1, regulates MCM function during prereplicative complex formation in DNA replication.The Journal of biological chemistry · 2013Article
- Article
- Promoter of a salinity and cold stress-induced MCM6 DNA helicase from pea.Plant signaling & behavior · 2011Article
- A single subunit MCM6 from pea promotes salinity stress tolerance without affecting yield.Plant molecular biology · 2011Article
- Inhibition of unwinding and ATPase activities of pea MCM6 DNA helicase by actinomycin and nogalamycin.Plant signaling & behavior · 2011Article
- MCM-BP regulates unloading of the MCM2-7 helicase in late S phase.Genes & development · 2011Article
- A single subunit MCM6 from pea forms homohexamer and functions as DNA helicase.Plant molecular biology · 2010Article
- The Saccharomyces cerevisiae Mcm6/2 and Mcm5/3 ATPase active sites contribute to the function of the putative Mcm2-7 'gate'.Nucleic acids research · 2010Article
- The effects of oligomerization on Saccharomyces cerevisiae Mcm4/6/7 function.BMC biochemistry · 2010Article
- Article
- The Mcm complex: unwinding the mechanism of a replicative helicase.Microbiology and molecular biology reviews : MMBR · 2009Review
- A biochemically active MCM-like helicase in Bacillus cereus.Nucleic acids research · 2009Article
- Dynamic localization of the DNA replication proteins MCM5 and MCM7 in plants.Plant physiology · 2009Article
- The minichromosome maintenance proteins 2-7 (MCM2-7) are necessary for RNA polymerase II (Pol II)-mediated transcription.The Journal of biological chemistry · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The replication fork helicase in eukaryotes is a large complex that is composed of Mcm2-7, Cdc45, and GINS. The Mcm2-7 proteins form a heterohexameric ring that hydrolyzes ATP and provide the motor function for this unwinding complex. A comprehensive study of how individual Mcm subunit biochemical activities relate to unwinding function has not been accomplished. We studied the mechanism of the Mcm4-Mcm6-Mcm7 complex, a useful model system because this complex has helicase activity in vitro. We separately purified each of three Mcm subunits until they were each nuclease-free, and we then examined the biochemical properties of different combinations of Mcm subunits. We found that Mcm4 and Mcm7 form an active unwinding assembly. The addition of Mcm6 to Mcm4/Mcm7 results in the formation of an active Mcm4/Mcm6/Mcm7 helicase assembly. The Mcm4-Mcm7 complex forms a ringed-shaped hexamer that unwinds DNA with 3' to 5' polarity by a steric exclusion mechanism, similar to Mcm4/Mcm6/Mcm7. The Mcm4-Mcm7 complex has a high level of ATPase activity that is further stimulated by DNA. The ability of different Mcm mixtures to form rings or exhibit DNA stimulation of ATPase activity correlates with the ability of these complexes to unwind DNA. The Mcm4/Mcm7 and Mcm4/Mcm6/Mcm7 assemblies can open to load onto circular DNA to initiate unwinding. We conclude that the Mcm subunits are surprisingly flexible and dynamic in their ability to interact with one another to form active unwinding complexes.
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