A Reversible Association between Smc Coiled Coils Is Regulated by Lysine Acetylation and Is Required for Cohesin Association with the DNA

A Reversible Association between Smc Coiled Coils Is Regulated by Lysine Acetylation and Is Required for Cohesin Association with the DNA
Title:
A Reversible Association between Smc Coiled Coils Is Regulated by Lysine Acetylation and Is Required for Cohesin Association with the DNA
Other Titles:
Molecular Cell
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Publication Date:
15 September 2016
Citation:
A Reversible Association between Smc Coiled Coils Is Regulated by Lysine Acetylation and Is Required for Cohesin Association with the DNA Kulemzina, Irina et al. Molecular Cell , Volume 63 , Issue 6 , 1044 - 1054
Abstract:
Cohesin is a ring-shaped protein complex that is capable of embracing DNA. Most of the ring circumference is comprised of the anti-parallel intramolecular coiled coils of the Smc1 and Smc3 proteins, which connect globular head and hinge domains. Smc coiled coil arms contain multiple acetylated and ubiquitylated lysines. To investigate the role of these modifications, we substituted lysines for arginines to mimic the unmodified state and uncovered genetic interaction between the Smc arms. Using scanning force microscopy, we show that wild-type Smc arms associate with each other when the complex is not on DNA. Deacetylation of the Smc1/Smc3 dimers promotes arms' dissociation. Smc arginine mutants display loose packing of the Smc arms and, although they dimerize at the hinges, fail to connect the heads and associate with the DNA. Our findings highlight the importance of a "collapsed ring," or "rod," conformation of cohesin for its loading on the chromosomes.
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PublisherCopyrights
Funding Info:
This work was supported by the Biomedical Research Council of A*STAR (Agency for Science, Technology and Research), Singapore Ministry of Education Academic Research Fund Tier 3 (MOE2012-T3-1-001) to J.Y., and the National Research Foundation of Singapore through the MechanobiologyInstitute at National University of Singapore to J.Y.
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Full paper can be downloaded from the Publisher's URL provided.
ISSN:
1097-2765
1097-4164
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