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Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation

Sister chromatid cohesion conferred by entrapment of sister DNAs within a tripartite ring formed between cohesin’s Scc1, Smc1, and Smc3 subunits is created during S and destroyed at anaphase through Scc1 cleavage by separase. Cohesin’s association with chromosomes is controlled by opposing activitie...

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Autores principales: Beckouët, Frederic, Srinivasan, Madhusudhan, Roig, Maurici Brunet, Chan, Kok-Lung, Scheinost, Johanna C., Batty, Paul, Hu, Bin, Petela, Naomi, Gligoris, Thomas, Smith, Alexandra C., Strmecki, Lana, Rowland, Benjamin D., Nasmyth, Kim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4769318/
https://www.ncbi.nlm.nih.gov/pubmed/26895425
http://dx.doi.org/10.1016/j.molcel.2016.01.026
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author Beckouët, Frederic
Srinivasan, Madhusudhan
Roig, Maurici Brunet
Chan, Kok-Lung
Scheinost, Johanna C.
Batty, Paul
Hu, Bin
Petela, Naomi
Gligoris, Thomas
Smith, Alexandra C.
Strmecki, Lana
Rowland, Benjamin D.
Nasmyth, Kim
author_facet Beckouët, Frederic
Srinivasan, Madhusudhan
Roig, Maurici Brunet
Chan, Kok-Lung
Scheinost, Johanna C.
Batty, Paul
Hu, Bin
Petela, Naomi
Gligoris, Thomas
Smith, Alexandra C.
Strmecki, Lana
Rowland, Benjamin D.
Nasmyth, Kim
author_sort Beckouët, Frederic
collection PubMed
description Sister chromatid cohesion conferred by entrapment of sister DNAs within a tripartite ring formed between cohesin’s Scc1, Smc1, and Smc3 subunits is created during S and destroyed at anaphase through Scc1 cleavage by separase. Cohesin’s association with chromosomes is controlled by opposing activities: loading by Scc2/4 complex and release by a separase-independent releasing activity as well as by cleavage. Coentrapment of sister DNAs at replication is accompanied by acetylation of Smc3 by Eco1, which blocks releasing activity and ensures that sisters remain connected. Because fusion of Smc3 to Scc1 prevents release and bypasses the requirement for Eco1, we suggested that release is mediated by disengagement of the Smc3/Scc1 interface. We show that mutations capable of bypassing Eco1 in Smc1, Smc3, Scc1, Wapl, Pds5, and Scc3 subunits reduce dissociation of N-terminal cleavage fragments of Scc1 (NScc1) from Smc3. This process involves interaction between Smc ATPase heads and is inhibited by Smc3 acetylation.
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spelling pubmed-47693182016-03-11 Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation Beckouët, Frederic Srinivasan, Madhusudhan Roig, Maurici Brunet Chan, Kok-Lung Scheinost, Johanna C. Batty, Paul Hu, Bin Petela, Naomi Gligoris, Thomas Smith, Alexandra C. Strmecki, Lana Rowland, Benjamin D. Nasmyth, Kim Mol Cell Article Sister chromatid cohesion conferred by entrapment of sister DNAs within a tripartite ring formed between cohesin’s Scc1, Smc1, and Smc3 subunits is created during S and destroyed at anaphase through Scc1 cleavage by separase. Cohesin’s association with chromosomes is controlled by opposing activities: loading by Scc2/4 complex and release by a separase-independent releasing activity as well as by cleavage. Coentrapment of sister DNAs at replication is accompanied by acetylation of Smc3 by Eco1, which blocks releasing activity and ensures that sisters remain connected. Because fusion of Smc3 to Scc1 prevents release and bypasses the requirement for Eco1, we suggested that release is mediated by disengagement of the Smc3/Scc1 interface. We show that mutations capable of bypassing Eco1 in Smc1, Smc3, Scc1, Wapl, Pds5, and Scc3 subunits reduce dissociation of N-terminal cleavage fragments of Scc1 (NScc1) from Smc3. This process involves interaction between Smc ATPase heads and is inhibited by Smc3 acetylation. Cell Press 2016-02-18 /pmc/articles/PMC4769318/ /pubmed/26895425 http://dx.doi.org/10.1016/j.molcel.2016.01.026 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Beckouët, Frederic
Srinivasan, Madhusudhan
Roig, Maurici Brunet
Chan, Kok-Lung
Scheinost, Johanna C.
Batty, Paul
Hu, Bin
Petela, Naomi
Gligoris, Thomas
Smith, Alexandra C.
Strmecki, Lana
Rowland, Benjamin D.
Nasmyth, Kim
Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title_full Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title_fullStr Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title_full_unstemmed Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title_short Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation
title_sort releasing activity disengages cohesin’s smc3/scc1 interface in a process blocked by acetylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4769318/
https://www.ncbi.nlm.nih.gov/pubmed/26895425
http://dx.doi.org/10.1016/j.molcel.2016.01.026
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