Structural Basis and IP6 Requirement for Pds5-Dependent Cohesin Dynamics.
Structural Basis and IP6 Requirement for Pds5-Dependent Cohesin Dynamics.
复制标题
DOI:
10.1016/j.molcel.2016.02.033
复制
发表时间:
2016-04-21
期刊:
影响因子:
16
通讯作者:
Yu H
中科院分区:
文献类型:
--
作者:
Ouyang Z;Zheng G;Tomchick DR;Luo X;Yu H
The ring-shaped cohesin complex regulates transcription, DNA repair, and chromosome segregation by dynamically entrapping chromosomes to promote chromosome compaction and sister-chromatid cohesion. The cohesin ring needs to open and close to allow its loading to and release from chromosomes. Cohesin dynamics are controlled by the releasing factors Pds5 and Wapl and the cohesin stabilizer Sororin. Here, we report the crystal structure of human Pds5B bound to a conserved peptide motif found in both Wapl and Sororin. Our structure establishes the basis for how Wapl and Sororin antagonistically influence cohesin dynamics. The structure further reveals that Pds5 can bind inositol hexakisphosphate (IP6). The IP6-binding segment of Pds5B is shaped like the jaw of a plier lever and inhibits the binding of Scc1 to Smc3. We propose that Pds5 stabilizes a transient, open state of cohesin to promote its release from chromosomes.
登录
查看更多内容
DOI:
10.1107/s090744491003982x
发表时间:
2011-04
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Evans PR
通讯作者:
Evans PR
影响因子:
7.5
作者:
Monserrate, Jessica P.;York, John D.
通讯作者:
York, John D.
影响因子:
9.2
作者:
Gerlich, Daniel;Koch, Birgit;Ellenberg, Jan
通讯作者:
Ellenberg, Jan
DOI:
10.1126/science.1256917
发表时间:
2014-11-21
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Gligoris TG;Scheinost JC;Bürmann F;Petela N;Chan KL;Uluocak P;Beckouët F;Gruber S;Nasmyth K;Löwe J
通讯作者:
Löwe J
影响因子:
64.8
作者:
Haering, Christian H.;Farcas, Ana-Maria;Nasmyth, Kim
通讯作者:
Nasmyth, Kim