Structure of an octameric form of the minichromosome maintenance protein from the archaeon Pyrococcus abyssi
|Author(s)||Cannone Giuseppe1, 2, 3, Visentin Silvia1, 2, 4, Palud Adeline5, 6, 7, Henneke Ghislaine5, 6, 7, Spagnolo Laura1|
|Affiliation(s)||1 : Univ Glasgow, Inst Mol Cell & Syst Biol, Univ Ave, Glasgow G12 8QQ, Lanark, Scotland.
2 : Sch Biol Sci, Edinburgh EH9 3JR, Midlothian, Scotland.
3 : Univ Edinburgh, Ctr Sci Extreme Condit, Edinburgh EH9 3JR, Midlothian, Scotland.
4 : Rutherford Appleton Labs, ISIS Neutron Source Sci & Technol Res Council, Harwell OX11 0QX, Berks, England.
5 : IFREMER, Lab Microbiol Environm Extremes, UMR 6197, Zi Pointe Diable CS 10070, F-29280 Plouzane, France.
6 : Univ Bretagne Occidentale, Lab Microbiol Environm Extremes, UMR 6197, Rue Dumont Urville, F-29280 Plouzane, France.
7 : CNRS, Lab Microbiol Environm Extremes, UMR 6197, Rue Dumont Urville, F-29280 Plouzane, France.
|Source||Scientific Reports (2045-2322) (Nature Publishing Group), 2017-02 , Vol. 7 , N. 42019 , P. 1-10|
|WOS© Times Cited||2|
|Abstract||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.|