How are cohesin rings opened and closed?

Shintomi, K., Hirano, T. (April 2007) How are cohesin rings opened and closed? Trends Biochem Sci, 32 (4). pp. 154-157. ISSN 0968-0004 (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/17320400
DOI: 10.1016/j.tibs.2007.02.002

Abstract

The cohesin complex is proposed to embrace sister chromatids within its ring-like structure, in which two ATP-binding 'head' domains of an SMC (structural maintenance of chromosomes) heterodimer are linked by a kleisin subunit. Recent studies shed new light on the crucial functions of the 'hinge' domain of the SMC dimer, which is located approximately 50nm from the head domains. An emerging idea is that the hinge and head domains cooperatively modulate cohesin-DNA interactions by opening and closing the ring in a highly regulated manner.

Item Type: Paper
Uncontrolled Keywords: NON-SMC SUBUNITS DNA INTERACTIONS ATP HYDROLYSIS CONDENSIN HINGE PROTEINS CHROMOSOMES ACTIVATION COMPLEX ARCHITECTURE
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cohesin complex
CSHL Authors:
Communities: CSHL labs > Hirano lab
Depositing User: CSHL Librarian
Date: April 2007
Date Deposited: 03 Nov 2011 19:24
Last Modified: 10 Apr 2018 16:06
Related URLs:
URI: http://repository.cshl.edu/id/eprint/23138

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