ATPase-dependent quality control of DNA replication origin licensing View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-03

AUTHORS

Jordi Frigola, Dirk Remus, Amina Mehanna, John F. X. Diffley

ABSTRACT

The regulated loading of the Mcm2-7 DNA helicase (comprising six related subunits, Mcm2 to Mcm7) into pre-replicative complexes at multiple replication origins ensures precise once per cell cycle replication in eukaryotic cells. The origin recognition complex (ORC), Cdc6 and Cdt1 load Mcm2-7 into a double hexamer bound around duplex DNA in an ATP-dependent reaction, but the molecular mechanism of this origin 'licensing' is still poorly understood. Here we show that both Mcm2-7 hexamers in Saccharomyces cerevisiae are recruited to origins by an essential, conserved carboxy-terminal domain of Mcm3 that interacts with and stimulates the ATPase activity of ORC-Cdc6. ATP hydrolysis can promote Mcm2-7 loading, but can also promote Mcm2-7 release if components are missing or if ORC has been inactivated by cyclin-dependent kinase phosphorylation. Our work provides new insights into how origins are licensed and reveals a novel ATPase-dependent mechanism contributing to precise once per cell cycle replication. More... »

PAGES

339

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature11920

DOI

http://dx.doi.org/10.1038/nature11920

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003048912

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23474987


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