Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi

Cannone, G., Visentin, S., Palud, A., Henneke, G. and Spagnolo, L. (2017) Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi. Scientific Reports, 7, 42019. (doi: 10.1038/srep42019) (PMID:28176822) (PMCID:PMC5296750)

133734.pdf - Published Version
Available under License Creative Commons Attribution.



Cell division is a complex process that requires precise duplication of genetic material. Duplication is concerted by replisomes. The Minichromosome Maintenance (MCM) replicative helicase is a crucial component of replisomes. Eukaryotic and archaeal MCM proteins are highly conserved. In fact, archaeal MCMs are powerful tools for elucidating essential features of MCM function. However, while eukaryotic MCM2-7 is a heterocomplex made of different polypeptide chains, the MCM complexes of many Archaea form homohexamers from a single gene product. Moreover, some archaeal MCMs are polymorphic, and both hexameric and heptameric architectures have been reported for the same polypeptide. Here, we present the structure of the archaeal MCM helicase from Pyrococcus abyssi in its single octameric ring assembly. To our knowledge, this is the first report of a full-length octameric MCM helicase.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Cannone, Dr Giuseppe and Spagnolo, Dr Laura
Authors: Cannone, G., Visentin, S., Palud, A., Henneke, G., and Spagnolo, L.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Scientific Reports
Publisher:Nature Publishing Group
ISSN (Online):2045-2322
Copyright Holders:Copyright © 2017 The Authors
First Published:First published in Scientific Reports 7:42019
Publisher Policy:Reproduced under a Creative Commons License

University Staff: Request a correction | Enlighten Editors: Update this record

Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
743381Elucidating the molecular architecture of the Archaeal CMR complex, a key player in the unicellular immune responseLaura SpagnoloBiotechnology and Biological Sciences Research Council (BBSRC)BB/J005673/2RI MOLECULAR CELL & SYSTEMS BIOLOGY