Xu, R. M. (June 2003) A pivotal role of the coiled coil of Sir4. Structure, 11 (6). pp. 608-609. ISSN 0969-2126
Abstract
The C terminus of Sir4 forms a coiled-coil structure. The coiled-coil domain is responsible for the dimerization of Sir4 and contains the binding site of Sir3. Structural and biochemical analyses of the Sir4 coiled-coil domain provide important insights into the molecular mechanisms of Sir3-Sir4 interaction and the assembly of a ternary Sir2/Sir3/Sir4 complex that are essential for epigenetic control of gene expression in S. cerevisiae.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | SACCHAROMYCES-CEREVISIAE TELOMERIC HETEROCHROMATIN SIR2/SIR4 COMPLEX YEAST BINDING |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function organism description > yeast |
| CSHL Authors: | |
| Communities: | CSHL labs > Xu lab |
| Depositing User: | Matt Covey |
| Date: | June 2003 |
| Date Deposited: | 11 Jun 2013 20:15 |
| Last Modified: | 11 Jun 2013 20:15 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/27936 |
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