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  Closing the cohesin ring: Structure and function of its Smc3-kleisin interface

Gligoris, T. G., Scheinost, J. C., Bürmann, F., Petela, N., Chan, K.-L., Uluocak, P., et al. (2014). Closing the cohesin ring: Structure and function of its Smc3-kleisin interface. SCIENCE, 346(6212), 963-967. doi:10.1126/science.1256917.

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 Creators:
Gligoris, Thomas G.1, Author
Scheinost, Johanna C.1, Author
Bürmann, Frank2, Author              
Petela, Naomi1, Author
Chan, Kok-Lung1, Author
Uluocak, Pelin1, Author
Beckouet, Frederic1, Author
Gruber, Stephan2, Author              
Nasmyth, Kim1, Author
Löwe, Jan1, Author
Affiliations:
1external, ou_persistent22              
2Gruber, Stephan / Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565151              

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Free keywords: SISTER-CHROMATID COHESION; ACETYLATION; COMPLEXES; PROTEIN; CHROMOSOMES; CLEAVAGE; PROPHASE; PROMOTES; SUBUNIT; WAPLScience & Technology - Other Topics;
 Abstract: Through their association with a kleisin subunit (Scc1), cohesin's Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid cohesion. Unlike the structure of Smc1/Smc3 and Smc1/Scc1 interfaces, that of Smc3/Scc1 is not known. Disconnection of this interface is thought to release cohesin from chromosomes in a process regulated by acetylation. We show here that the N-terminal domain of yeast Sccl contains two alpha helices, forming a four-helix bundle with the coiled coil emerging from Smc3's adenosine triphosphatase head. Mutations affecting this interaction compromise cohesin's association with chromosomes. The interface is far from Smc3 residues, whose acetylation prevents cohesin's dissociation from chromosomes. Cohesin complexes holding chromatids together in vivo do indeed have the configuration of hetero-trimeric rings, and sister DNAs are entrapped within these.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000345696000035
DOI: 10.1126/science.1256917
 Degree: -

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Title: SCIENCE
Source Genre: Journal
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Publ. Info: 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA : AMER ASSOC ADVANCEMENT SCIENCE
Pages: - Volume / Issue: 346 (6212) Sequence Number: - Start / End Page: 963 - 967 Identifier: ISSN: 0036-8075