Conserved disruptions in the predicted coiled-coil domains of eukaryotic SMC complexes: Implications for structure and function.

Beasley, M, Xu, H, Warren, WD, and McKay, MJ (2002) Conserved disruptions in the predicted coiled-coil domains of eukaryotic SMC complexes: Implications for structure and function. Genome research, 12 (8). pp. 1201-1209.

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Abstract

The structural maintenance of chromosome (SMC) proteins are required for a number of essential nuclear processes, including those of chromosome condensation, chromatid cohesion, and DNA repair. Eukaryotic SMC proteins form heterodimers capable of binding DNA and possess a DNA-stimulated ATPase activity. They have a characteristic structure of terminal globular domains with two internal arms that are predicted to form a coiled-coil structure interspaced with a globular "hinge" domain. We report here that the predicted coiled-coil arms are disrupted at conserved sites in SMC proteins. These disruptions, which vary in length and sequence identity, abolish the otherwise symmetrical secondary structure of antiparallel SMC heterodimers and provide the first evidence for a possible functional orientation of eukaryotic SMC complexes. The retention of these breaks between evolutionarily distant, yet related, SMC members indicates that they may have a fundamental role in SMC heterodimer function.

Item ID: 1006
Item Type: Article (UNSPECIFIED)
Keywords: Cohesin, SMC, Chromosome cohesion
Additional Information:

Copyright © 2002, Genome Research Online by Cold Spring Harbor Laboratory Press.

ISSN: 1549-5469
Date Deposited: 03 Nov 2006
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060103 Cell Development, Proliferation and Death @ 0%
06 BIOLOGICAL SCIENCES > 0604 Genetics > 060403 Developmental Genetics (incl Sex Determination) @ 0%
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