The structural basis for MCM2–7 helicase activation by GINS and Cdc45 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-04

AUTHORS

Alessandro Costa, Ivar Ilves, Nele Tamberg, Tatjana Petojevic, Eva Nogales, Michael R Botchan, James M Berger

ABSTRACT

Two central steps for initiating eukaryotic DNA replication involve loading of the Mcm2-7 helicase onto double-stranded DNA and its activation by GINS-Cdc45. To better understand these events, we determined the structures of Mcm2-7 and the CMG complex by using single-particle electron microscopy. Mcm2-7 adopts two conformations--a lock-washer-shaped spiral state and a planar, gapped-ring form--in which Mcm2 and Mcm5 flank a breach in the helicase perimeter. GINS and Cdc45 bridge this gap, forming a topologically closed assembly with a large interior channel; nucleotide binding further seals off the discontinuity between Mcm2 and Mcm5, partitioning the channel into two smaller pores. Together, our data help explain how GINS and Cdc45 activate Mcm2-7, indicate that Mcm2-7 loading may be assisted by a natural predisposition of the hexamer to form open rings, and suggest a mechanism by which the CMG complex assists DNA strand separation. More... »

PAGES

471

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.2004

DOI

http://dx.doi.org/10.1038/nsmb.2004

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038111337

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21378962


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