Reactome | Mcm4,6,7 trimer forms and associates with the replication fork

Mcm4,6,7 trimer forms and associates with the replication fork

Stable Identifier

R-HSA-69019

Type

Reaction [dissociation]

Species

Homo sapiens

Compartment

nucleoplasm

Synonyms

Rearrangement and mobilization of Mcm2-7

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Mcm4,6,7 trimer forms and associates with the replication fork

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

At the start of the elongation phase of DNA replication, the Mcm2-7 complex may re-arrange to function as the replicative helicase associated with the replication fork. In general, a replicative helicase is associated with the replication fork and unwinds DNA ahead of the polymerase. In yeast, the Mcm proteins associate with origin DNA in G1 phase and then exit the origin upon replication initiation, consistent with moving out of the origin with the replication fork. The Mcm2-7 complex is a ring-shaped hexamer. Complexes of Mcm4, Mcm6 and Mcm7 proteins from humans or S. pombe display a modest ATP-dependent helicase activity in vitro. Consistent with the hypothesis that eukaryotic Mcm complexes function as helicases, an archaeal Mcm homolog is a ring-shaped double hexamer that has a processive DNA unwinding activity. Mcm proteins may have additional functions during elongation, as uninterrupted function of all six is required for replication fork progression in budding yeast. Mcm4,6,7 helicase activity may be negatively regulated in two ways. Mcm2, Mcm4, Mcm6, and Mcm7 also form a stable complex which, however, has no helicase activity, suggesting that Mcm2 inhibits DNA unwinding by Mcm4,6,7. In addition, phosphorylation of human Mcm4,6,7 complex by CDK inhibits its helicase activity.

Literature References

PubMed ID	Title	Journal	Year
10884341	Electron microscopic observation and single-stranded DNA binding activity of the Mcm4,6,7 complex. Sato, M, Gotow, T, You, Z, Komamura-Kohno, Y, Uchiyama, Y, Yabuta, N, Nojima, H, Ishimi, Y	J Mol Biol	2000
12364596	Human Mcm proteins at a replication origin during the G1 to S phase transition. Schaarschmidt, D, Ladenburger, EM, Keller, C, Knippers, R	Nucleic Acids Res	2002