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The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes

The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes AbstractStructural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization ‘hinge’. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png FEMS Microbiology Reviews Oxford University Press

The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes

FEMS Microbiology Reviews , Volume 38 (3) – May 1, 2014

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References (96)

Publisher
Oxford University Press
Copyright
© 2014 Federation of European Microbiological Societies.
ISSN
0168-6445
eISSN
1574-6976
DOI
10.1111/1574-6976.12045
pmid
24118085
Publisher site
See Article on Publisher Site

Abstract

AbstractStructural Maintenance of Chromosomes (SMC) protein complexes are found in all three domains of life. They are characterized by a distinctive and conserved architecture in which a globular ATPase ‘head’ domain is formed by the N- and C-terminal regions of the SMC protein coming together, with a c. 50-nm-long antiparallel coiled-coil separating the head from a dimerization ‘hinge’. Dimerization gives both V- and O-shaped SMC dimers. The distinctive architecture points to a conserved biochemical mechanism of action. However, the details of this mechanism are incomplete, and the precise ways in which this mechanism leads to the biological functions of these complexes in chromosome organization and processing remain unclear. In this review, we introduce the properties of bacterial SMC complexes, compare them with eukaryotic complexes and discuss how their likely biochemical action relates to their roles in chromosome organization and segregation.

Journal

FEMS Microbiology ReviewsOxford University Press

Published: May 1, 2014

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