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Impairing Cohesin Smc1/3 Head Engagement Compensates for the Lack of Eco1 Function

Huber, Roland G. ; Kulemzina, Irina ; Ang, Keven ; Chavda, Alap P. ; Suranthran, Sasikala ; Teh, Jun Thing ; Kenanov, Dimitar ; Liu, Gaowen ; Rancati, Giulia and Szmyd, Radoslaw , et al. (2016) In Structure 24(11). p.1991-1999
Abstract

The cohesin ring, which is composed of the Smc1, Smc3, and Scc1 subunits, topologically embraces two sister chromatids from S phase until anaphase to ensure their precise segregation to the daughter cells. The opening of the ring is required for its loading on the chromosomes and unloading by the action of Wpl1 protein. Both loading and unloading are dependent on ATP hydrolysis by the Smc1 and Smc3 “head” domains, which engage to form two composite ATPase sites. Based on the available structures, we modeled the Saccharomyces cerevisiae Smc1/Smc3 head heterodimer and discovered that the Smc1/Smc3 interfaces at the two ATPase sites differ in the extent of protein contacts and stability after ATP hydrolysis. We identified smc1 and smc3... (More)

The cohesin ring, which is composed of the Smc1, Smc3, and Scc1 subunits, topologically embraces two sister chromatids from S phase until anaphase to ensure their precise segregation to the daughter cells. The opening of the ring is required for its loading on the chromosomes and unloading by the action of Wpl1 protein. Both loading and unloading are dependent on ATP hydrolysis by the Smc1 and Smc3 “head” domains, which engage to form two composite ATPase sites. Based on the available structures, we modeled the Saccharomyces cerevisiae Smc1/Smc3 head heterodimer and discovered that the Smc1/Smc3 interfaces at the two ATPase sites differ in the extent of protein contacts and stability after ATP hydrolysis. We identified smc1 and smc3 mutations that disrupt one of the interfaces and block the Wpl1-mediated release of cohesin from DNA. Thus, we provide structural insights into how the cohesin heads engage with each other.

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publishing date
type
Contribution to journal
publication status
published
keywords
cohesin, molecular dynamics simulation, protein-protein interactions, sister chromatid cohesion
in
Structure
volume
24
issue
11
pages
1991 - 1999
publisher
Cell Press
external identifiers
  • pmid:27692962
  • scopus:84994337306
ISSN
0969-2126
DOI
10.1016/j.str.2016.09.001
language
English
LU publication?
no
id
daae7f41-7bc7-4fdb-9dca-ddd3ed0da143
date added to LUP
2019-09-18 13:44:18
date last changed
2020-11-22 04:00:55
@article{daae7f41-7bc7-4fdb-9dca-ddd3ed0da143,
  abstract     = {<p>The cohesin ring, which is composed of the Smc1, Smc3, and Scc1 subunits, topologically embraces two sister chromatids from S phase until anaphase to ensure their precise segregation to the daughter cells. The opening of the ring is required for its loading on the chromosomes and unloading by the action of Wpl1 protein. Both loading and unloading are dependent on ATP hydrolysis by the Smc1 and Smc3 “head” domains, which engage to form two composite ATPase sites. Based on the available structures, we modeled the Saccharomyces cerevisiae Smc1/Smc3 head heterodimer and discovered that the Smc1/Smc3 interfaces at the two ATPase sites differ in the extent of protein contacts and stability after ATP hydrolysis. We identified smc1 and smc3 mutations that disrupt one of the interfaces and block the Wpl1-mediated release of cohesin from DNA. Thus, we provide structural insights into how the cohesin heads engage with each other.</p>},
  author       = {Huber, Roland G. and Kulemzina, Irina and Ang, Keven and Chavda, Alap P. and Suranthran, Sasikala and Teh, Jun Thing and Kenanov, Dimitar and Liu, Gaowen and Rancati, Giulia and Szmyd, Radoslaw and Kaldis, Philipp and Bond, Peter J. and Ivanov, Dmitri},
  issn         = {0969-2126},
  language     = {eng},
  month        = {11},
  number       = {11},
  pages        = {1991--1999},
  publisher    = {Cell Press},
  series       = {Structure},
  title        = {Impairing Cohesin Smc1/3 Head Engagement Compensates for the Lack of Eco1 Function},
  url          = {http://dx.doi.org/10.1016/j.str.2016.09.001},
  doi          = {10.1016/j.str.2016.09.001},
  volume       = {24},
  year         = {2016},
}