Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity

[EN] Replication fork stability is challenged in conditions of replication stress and protected by the Mec1/ATR checkpoint to preserve genome integrity. An enigmatic role in fork protection is played by cohesin, which mediates key chromosome transactions by topologically entrapping DNA. Searching fo...

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Detalhes bibliográficos
Autor: Villa Hernández, Sara
Tipo de documento: tese
Data de publicação:2016
País:España
Recursos:Universidad de Salamanca (USAL)
Repositório:GREDOS. Repositorio Institucional de la Universidad de Salamanca
OAI Identifier:oai:gredos.usal.es:10366/133097
Acesso em linha:http://hdl.handle.net/10366/133097
Access Level:Acceso aberto
Palavra-chave:Tesis y disertaciones académicas
Universidad de Salamanca (España)
Resumen de tesis
Thesis Abstracts
Biología molecular
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spelling Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrityCohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrityVilla Hernández, SaraTesis y disertaciones académicasUniversidad de Salamanca (España)Resumen de tesisThesis AbstractsBiología molecular[EN] Replication fork stability is challenged in conditions of replication stress and protected by the Mec1/ATR checkpoint to preserve genome integrity. An enigmatic role in fork protection is played by cohesin, which mediates key chromosome transactions by topologically entrapping DNA. Searching for factors interfacing with the checkpoint response, we found that the Rsp5Bul2 ubiquitin ligase promotes stalled fork progression. Rsp5Bul2 physically interacts with cohesin and the Mec1 kinase, thus mediating checkpoint-dependent cohesin ubiquitylation and stimulating cohesin function in fork protection. The Cdc48/p97 ubiquitin selective segregase, together with Rsp5Bul2, promotes cohesin dissociation from replicating chromatin. Mobilization by Cdc48 involves Wpl1 function and is required for cohesin relocation to newly synthesized chromatids and replication stress survival. Cohesin-mediated fork protection also relies on Eco1, which secures sister chromatid entrapment. The results here presented indicate that ubiquitylation facilitates cohesin interfacing with stalled forks to protect fork-replisome dynamic architecture and sustain replication progression.Bermejo Moreno, RodrigoSegurado Carrascal, Mónica201720172016info:eu-repo/semantics/doctoralThesisapplication/pdfhttp://hdl.handle.net/10366/133097reponame:GREDOS. Repositorio Institucional de la Universidad de Salamancainstname:Universidad de Salamanca (USAL)EspañolAttribution-NonCommercial-NoDerivs 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:gredos.usal.es:10366/1330972026-06-07T06:28:51Z
dc.title.none.fl_str_mv Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
title Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
spellingShingle Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
Villa Hernández, Sara
Tesis y disertaciones académicas
Universidad de Salamanca (España)
Resumen de tesis
Thesis Abstracts
Biología molecular
title_short Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
title_full Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
title_fullStr Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
title_full_unstemmed Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
title_sort Resumen de tesis. Cohesin Ubiquitylation and Mobilisation by an Rsp5/bul2 - cdc48axis facilitate stalled fork dynamics and integrity
dc.creator.none.fl_str_mv Villa Hernández, Sara
author Villa Hernández, Sara
author_facet Villa Hernández, Sara
author_role author
dc.contributor.none.fl_str_mv Bermejo Moreno, Rodrigo
Segurado Carrascal, Mónica
dc.subject.none.fl_str_mv Tesis y disertaciones académicas
Universidad de Salamanca (España)
Resumen de tesis
Thesis Abstracts
Biología molecular
topic Tesis y disertaciones académicas
Universidad de Salamanca (España)
Resumen de tesis
Thesis Abstracts
Biología molecular
description [EN] Replication fork stability is challenged in conditions of replication stress and protected by the Mec1/ATR checkpoint to preserve genome integrity. An enigmatic role in fork protection is played by cohesin, which mediates key chromosome transactions by topologically entrapping DNA. Searching for factors interfacing with the checkpoint response, we found that the Rsp5Bul2 ubiquitin ligase promotes stalled fork progression. Rsp5Bul2 physically interacts with cohesin and the Mec1 kinase, thus mediating checkpoint-dependent cohesin ubiquitylation and stimulating cohesin function in fork protection. The Cdc48/p97 ubiquitin selective segregase, together with Rsp5Bul2, promotes cohesin dissociation from replicating chromatin. Mobilization by Cdc48 involves Wpl1 function and is required for cohesin relocation to newly synthesized chromatids and replication stress survival. Cohesin-mediated fork protection also relies on Eco1, which secures sister chromatid entrapment. The results here presented indicate that ubiquitylation facilitates cohesin interfacing with stalled forks to protect fork-replisome dynamic architecture and sustain replication progression.
publishDate 2016
dc.date.none.fl_str_mv 2016
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/doctoralThesis
format doctoralThesis
dc.identifier.none.fl_str_mv http://hdl.handle.net/10366/133097
url http://hdl.handle.net/10366/133097
dc.language.none.fl_str_mv Español
language_invalid_str_mv Español
dc.rights.none.fl_str_mv Attribution-NonCommercial-NoDerivs 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Attribution-NonCommercial-NoDerivs 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:GREDOS. Repositorio Institucional de la Universidad de Salamanca
instname:Universidad de Salamanca (USAL)
instname_str Universidad de Salamanca (USAL)
reponame_str GREDOS. Repositorio Institucional de la Universidad de Salamanca
collection GREDOS. Repositorio Institucional de la Universidad de Salamanca
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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