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

被引：24

作者：

Kulemzina, Irina ^{[1
,3
]}

Ang, Keven ^{[1
]}

Zhao, Xiaodan ^{[4
]}

Teh, Jun-Thing ^{[1
]}

Verma, Vikash ^{[3
,9
]}

Suranthran, Sasikala ^{[1
]}

Chavda, Alap P. ^{[1
]}

Huber, Roland G. ^{[1
]}

Eisenhaber, Birgit ^{[1
]}

Eisenhaber, Frank ^{[1
,7
,8
]}

Yan, Jie ^{[4
,5
,6
]}

Ivanov, Dmitri ^{[1
,2
,3
,5
]}

机构：

[1] ASTAR, Bioinformat Inst, Singapore 138671, Singapore

[2] ASTAR, Inst Mol & Cell Biol, Singapore 138673, Singapore

[3] Max Planck Gesell, Friedrich Miescher Lab, D-72076 Tubingen, Germany

[4] Natl Univ Singapore, Mechanobiol Inst, Singapore 117411, Singapore

[5] Natl Univ Singapore, Dept Phys, Singapore 117551, Singapore

[6] Natl Univ Singapore, Ctr Bioimaging Sci, Singapore 117557, Singapore

[7] Nanyang Technol Univ, Sch Comp Engn, Singapore 637553, Singapore

[8] Natl Univ Singapore, Dept Biol Sci, Singapore 117597, Singapore

[9] Univ Michigan, Dept Cell & Dev Biol, Ann Arbor, MI 48109 USA

来源：

MOLECULAR CELL | 2016年 / 63卷 / 06期

基金：

新加坡国家研究基金会;

关键词：

ATP HYDROLYSIS; EXIT GATE; CONDENSIN; BINDING; COMPLEX; RING; ARCHITECTURE; CHROMOSOMES; MUTATIONS; YEAST;

D O I：

10.1016/j.molcel.2016.08.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1044 / 1054

页数：11

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