Cargando…

Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening

Cohesin stably holds together the sister chromatids from S phase until mitosis. To do so, cohesin must be protected against its cellular antagonist Wapl. Eco1 acetylates cohesin’s Smc3 subunit, which locks together the sister DNAs. We used yeast genetics to dissect how Wapl drives cohesin from chrom...

Descripción completa

Detalles Bibliográficos
Autores principales: Elbatsh, Ahmed M.O., Haarhuis, Judith H.I., Petela, Naomi, Chapard, Christophe, Fish, Alexander, Celie, Patrick H., Stadnik, Magda, Ristic, Dejan, Wyman, Claire, Medema, René H., Nasmyth, Kim, Rowland, Benjamin D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4769319/
https://www.ncbi.nlm.nih.gov/pubmed/26895426
http://dx.doi.org/10.1016/j.molcel.2016.01.025
_version_ 1782418086569181184
author Elbatsh, Ahmed M.O.
Haarhuis, Judith H.I.
Petela, Naomi
Chapard, Christophe
Fish, Alexander
Celie, Patrick H.
Stadnik, Magda
Ristic, Dejan
Wyman, Claire
Medema, René H.
Nasmyth, Kim
Rowland, Benjamin D.
author_facet Elbatsh, Ahmed M.O.
Haarhuis, Judith H.I.
Petela, Naomi
Chapard, Christophe
Fish, Alexander
Celie, Patrick H.
Stadnik, Magda
Ristic, Dejan
Wyman, Claire
Medema, René H.
Nasmyth, Kim
Rowland, Benjamin D.
author_sort Elbatsh, Ahmed M.O.
collection PubMed
description Cohesin stably holds together the sister chromatids from S phase until mitosis. To do so, cohesin must be protected against its cellular antagonist Wapl. Eco1 acetylates cohesin’s Smc3 subunit, which locks together the sister DNAs. We used yeast genetics to dissect how Wapl drives cohesin from chromatin and identified mutants of cohesin that are impaired in ATPase activity but remarkably confer robust cohesion that bypasses the need for the cohesin protectors Eco1 in yeast and Sororin in human cells. We uncover a functional asymmetry within the heart of cohesin’s highly conserved ABC-like ATPase machinery and find that both ATPase sites contribute to DNA loading, whereas DNA release is controlled specifically by one site. We propose that Smc3 acetylation locks cohesin rings around the sister chromatids by counteracting an activity associated with one of cohesin’s two ATPase sites.
format Online
Article
Text
id pubmed-4769319
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Cell Press
record_format MEDLINE/PubMed
spelling pubmed-47693192016-03-11 Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening Elbatsh, Ahmed M.O. Haarhuis, Judith H.I. Petela, Naomi Chapard, Christophe Fish, Alexander Celie, Patrick H. Stadnik, Magda Ristic, Dejan Wyman, Claire Medema, René H. Nasmyth, Kim Rowland, Benjamin D. Mol Cell Article Cohesin stably holds together the sister chromatids from S phase until mitosis. To do so, cohesin must be protected against its cellular antagonist Wapl. Eco1 acetylates cohesin’s Smc3 subunit, which locks together the sister DNAs. We used yeast genetics to dissect how Wapl drives cohesin from chromatin and identified mutants of cohesin that are impaired in ATPase activity but remarkably confer robust cohesion that bypasses the need for the cohesin protectors Eco1 in yeast and Sororin in human cells. We uncover a functional asymmetry within the heart of cohesin’s highly conserved ABC-like ATPase machinery and find that both ATPase sites contribute to DNA loading, whereas DNA release is controlled specifically by one site. We propose that Smc3 acetylation locks cohesin rings around the sister chromatids by counteracting an activity associated with one of cohesin’s two ATPase sites. Cell Press 2016-02-18 /pmc/articles/PMC4769319/ /pubmed/26895426 http://dx.doi.org/10.1016/j.molcel.2016.01.025 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
Elbatsh, Ahmed M.O.
Haarhuis, Judith H.I.
Petela, Naomi
Chapard, Christophe
Fish, Alexander
Celie, Patrick H.
Stadnik, Magda
Ristic, Dejan
Wyman, Claire
Medema, René H.
Nasmyth, Kim
Rowland, Benjamin D.
Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title_full Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title_fullStr Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title_full_unstemmed Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title_short Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening
title_sort cohesin releases dna through asymmetric atpase-driven ring opening
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4769319/
https://www.ncbi.nlm.nih.gov/pubmed/26895426
http://dx.doi.org/10.1016/j.molcel.2016.01.025
work_keys_str_mv AT elbatshahmedmo cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT haarhuisjudithhi cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT petelanaomi cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT chapardchristophe cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT fishalexander cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT celiepatrickh cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT stadnikmagda cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT risticdejan cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT wymanclaire cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT medemareneh cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT nasmythkim cohesinreleasesdnathroughasymmetricatpasedrivenringopening
AT rowlandbenjamind cohesinreleasesdnathroughasymmetricatpasedrivenringopening