SMC proteins and chromosome mechanics: from bacteria to humans

Hirano, T. (March 2005) SMC proteins and chromosome mechanics: from bacteria to humans. Philos Trans R Soc Lond B Biol Sci, 360 (1455). pp. 507-14. ISSN 0962-8436 (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/15897176
DOI: 10.1098/rstb.2004.1606

Abstract

Chromosome cohesion and condensation are essential prerequisites of proper segregation of genomes during mitosis and meiosis, and are supported by two structurally related protein complexes, cohesin and condensin, respectively. At the core of the two complexes lie members of the structural maintenance of chromosomes (SMC) family of ATPases. SMC proteins are also found in most bacterial and archaeal species, implicating the existence of an evolutionarily conserved theme of higher-order chromosome organization and dynamics. SMC dimers adopt a two-armed structure with an ATP-binding cassette (ABC)-like domain at the distal end of each arm. This article reviews recent work on the bacterial and eukaryotic SMC protein complexes, and discusses current understanding of how these uniquely designed protein machines may work at a mechanistic level. It seems most likely that the action of SMC proteins is highly dynamic and plastic, possibly involving a diverse array of intramolecular and intermolecular protein-protein interactions.

Item Type: Paper
Uncontrolled Keywords: Adenosine Triphosphatases physiology Animals Bacterial Physiology Cell Cycle physiology Cell Cycle Proteins Chromosomal Proteins Non-Histone metabolism physiology Chromosome Segregation physiology DNA-Binding Proteins physiology Eukaryotic Cells physiology Evolution Molecular Fungal Proteins Humans Models Biological Multiprotein Complexes metabolism physiology Nuclear Proteins physiology
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > condensin complex
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: CSHL Librarian
Date: 29 March 2005
Date Deposited: 12 Jan 2012 19:46
Last Modified: 07 May 2018 15:22
PMCID: PMC1569466
Related URLs:
URI: https://repository.cshl.edu/id/eprint/22597

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