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

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 t...

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Published in:	Science (American Association for the Advancement of Science) Vol. 346; no. 6212; pp. 963 - 967
Main Authors:	Gligoris, Thomas G., Scheinost, Johanna C., Bürmann, Frank, Petela, Naomi, Chan, Kok-Lung, Uluocak, Pelin, Beckouët, Frédéric, Gruber, Stephan, Nasmyth, Kim, Löwe, Jan
Format:	Journal Article
Language:	English
Published:	United States American Association for the Advancement of Science 21-11-2014 The American Association for the Advancement of Science
Subjects:	Acetylation Adenosine triphosphatase Adenosine triphosphatases Adenosine Triphosphatases - chemistry Amino Acid Sequence Bundling Cell Cycle Proteins - chemistry Cell Cycle Proteins - genetics Chromatids Chromatin Chromosomal Proteins, Non-Histone - chemistry Chromosomal Proteins, Non-Histone - genetics Chromosomes Circles Cohesins Cohesion Coiling Conserved Sequence Cross-Linking Reagents - chemistry Crystal structure Crystallography, X-Ray Deoxyribonucleic acid Dimers DNA DNA - chemistry Immunoprecipitation Mathematical rings Molecules Mutation Mutations Protein Multimerization Protein Structure, Tertiary Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Strands Yeast
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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 Scc1 contains two α 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.
AbstractList	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 (NTD) of yeast Scc1 contains two α helices, forming a four helix bundle with the coiled coil emerging from Smc3’s ATPase 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. 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 Scc1 contains two α 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. Holding together homologous sister chromosome pairs is a vital requirement during cell division and DNA repair. A special complex, called cohesin, forms a ring made of three different proteins and functions to hold together the two sister DNA strands. Gligoris et al. and Huis in 't Veld et al. identified a specific protein-protein interface within the cohesin ring that forms a DNA exit gate. Mutations in this interface prevented cohesion between sister chromatids. Thus, the cohesin ring must indeed encircle the two DNA strands to hold them together. Science, this issue p. 963, p. 968 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 Scc1 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. A cohesin ring around two DNA strandsHolding together homologous sister chromosome pairs is a vital requirement during cell division and DNA repair. A special complex, called cohesin, forms a ring made of three different proteins and functions to hold together the two sister DNA strands. Gligoris et al. and Huis in 't Veld et al. identified a specific protein-protein interface within the cohesin ring that forms a DNA exit gate. Mutations in this interface prevented cohesion between sister chromatids. Thus, the cohesin ring must indeed encircle the two DNA strands to hold them together.Science, this issue p. 963, p. 968 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 Scc1 contains two α 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. 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 Scc1 contains two α 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. The presence of a DNA “exit gate” in a tripartite ring of proteins confirms that the ring holds together sister chromatid DNA strands. Holding together homologous sister chromosome pairs is a vital requirement during cell division and DNA repair. A special complex, called cohesin, forms a ring made of three different proteins and functions to hold together the two sister DNA strands. Gligoris et al. and Huis in 't Veld et al. identified a specific protein-protein interface within the cohesin ring that forms a DNA exit gate. Mutations in this interface prevented cohesion between sister chromatids. Thus, the cohesin ring must indeed encircle the two DNA strands to hold them together. Science , this issue p. 963 , p. 968
Author	Petela, Naomi Beckouët, Frédéric Gruber, Stephan Scheinost, Johanna C. Nasmyth, Kim Chan, Kok-Lung Uluocak, Pelin Löwe, Jan Gligoris, Thomas G. Bürmann, Frank
AuthorAffiliation	3 Max-Planck-Institut für Biochemie, 82152, Martinsried, Germany 2 Dunn School of Pathology, University of Oxford, OX1 3RF, United Kingdom 1 Department of Biochemistry, University of Oxford, OX1 3QU, United Kingdom 4 MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom
AuthorAffiliation_xml	– name: 4 MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom – name: 2 Dunn School of Pathology, University of Oxford, OX1 3RF, United Kingdom – name: 1 Department of Biochemistry, University of Oxford, OX1 3QU, United Kingdom – name: 3 Max-Planck-Institut für Biochemie, 82152, Martinsried, Germany
Author_xml	– sequence: 1 givenname: Thomas G. surname: Gligoris fullname: Gligoris, Thomas G. – sequence: 2 givenname: Johanna C. surname: Scheinost fullname: Scheinost, Johanna C. – sequence: 3 givenname: Frank surname: Bürmann fullname: Bürmann, Frank – sequence: 4 givenname: Naomi surname: Petela fullname: Petela, Naomi – sequence: 5 givenname: Kok-Lung surname: Chan fullname: Chan, Kok-Lung – sequence: 6 givenname: Pelin surname: Uluocak fullname: Uluocak, Pelin – sequence: 7 givenname: Frédéric surname: Beckouët fullname: Beckouët, Frédéric – sequence: 8 givenname: Stephan surname: Gruber fullname: Gruber, Stephan – sequence: 9 givenname: Kim surname: Nasmyth fullname: Nasmyth, Kim – sequence: 10 givenname: Jan surname: Löwe fullname: Löwe, Jan
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/25414305$$D View this record in MEDLINE/PubMed
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Snippet	Through their association with a kleisin subunit (Scc1), cohesin's Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid... Through their association with a kleisin subunit (Scc1), cohesin’s Smc1 and Smc3 subunits are thought to form tripartite rings that mediate sister chromatid...
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SubjectTerms	Acetylation Adenosine triphosphatase Adenosine triphosphatases Adenosine Triphosphatases - chemistry Amino Acid Sequence Bundling Cell Cycle Proteins - chemistry Cell Cycle Proteins - genetics Chromatids Chromatin Chromosomal Proteins, Non-Histone - chemistry Chromosomal Proteins, Non-Histone - genetics Chromosomes Circles Cohesins Cohesion Coiling Conserved Sequence Cross-Linking Reagents - chemistry Crystal structure Crystallography, X-Ray Deoxyribonucleic acid Dimers DNA DNA - chemistry Immunoprecipitation Mathematical rings Molecules Mutation Mutations Protein Multimerization Protein Structure, Tertiary Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Strands Yeast
Title	Closing the cohesin ring: Structure and function of its Smc3-kleisin interface
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