Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-09

AUTHORS

Adam T McGeoch, Michael A Trakselis, Ronald A Laskey, Stephen D Bell

ABSTRACT

The homomultimeric archaeal mini-chromosome maintenance (MCM) complex serves as a simple model for the analogous heterohexameric eukaryotic complex. Here we investigate the organization and orientation of the MCM complex of the hyperthermophilic archaeon Sulfolobus solfataricus (Sso) on model DNA substrates. Sso MCM binds as a hexamer and slides on the end of a 3'-extended single-stranded DNA tail of a Y-shaped substrate; binding is oriented so that the motor domain of the protein faces duplex DNA. Two candidate beta-hairpin motifs within the MCM monomer have partially redundant roles in DNA binding. Notably, however, conserved basic residues within these motifs have nonequivalent roles in the helicase activity of MCM. On the basis of these findings, we propose a model for the mechanism of the helicase activity of MCM and note parallels with SV40 T antigen. More... »

PAGES

756-762

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb974

DOI

http://dx.doi.org/10.1038/nsmb974

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034811191

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16116441


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