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)
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: | https://repository.cshl.edu/id/eprint/23138 |
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