Smc5/6, an atypical SMC complex with two RING-type subunits

Smc5/6, an atypical SMC complex with two RING-type subunits Roger Solé-Soler ; Jordi Torres-Rosell Crossmark: Check for Updates Biochem Soc Trans (2020) 48 (5): 2159-2171. https://doi.org/10.1042/BST20200389 Article history Share Icon Share Cite Icon Cite Get Permissions The Smc5/6 complex plays ess...

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Detalles Bibliográficos
Autores: Solé-Soler, Roger, Torres Rosell, Jordi
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10459.1/70771
Acceso en línea:https://doi.org/10.1042/BST20200389
http://hdl.handle.net/10459.1/70771
Access Level:acceso abierto
Palabra clave:Chromosomes
E3 ligases
SMC complex
Smc5/6
SUMO
Ubiquitin
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spelling Smc5/6, an atypical SMC complex with two RING-type subunitsSolé-Soler, RogerTorres Rosell, JordiChromosomesE3 ligasesSMC complexSmc5/6SUMOUbiquitinSmc5/6, an atypical SMC complex with two RING-type subunits Roger Solé-Soler ; Jordi Torres-Rosell Crossmark: Check for Updates Biochem Soc Trans (2020) 48 (5): 2159-2171. https://doi.org/10.1042/BST20200389 Article history Share Icon Share Cite Icon Cite Get Permissions The Smc5/6 complex plays essential roles in chromosome segregation and repair, by promoting disjunction of sister chromatids. The core of the complex is constituted by an heterodimer of Structural Maintenance of Chromosomes (SMC) proteins that use ATP hydrolysis to dynamically associate with and organize chromosomes. In addition, the Smc5/6 complex contains six non-SMC subunits. Remarkably, and differently to other SMC complexes, the Nse1 and Nse2 subunits contain RING-type domains typically found in E3 ligases, pointing to the capacity to regulate other proteins and complexes through ubiquitin-like modifiers. Nse2 codes for a C-terminal SP-RING domain with SUMO ligase activity, assisting Smc5/6 functions in chromosome segregation through sumoylation of several chromosome-associated proteins. Nse1 codes for a C-terminal NH-RING domain and, although it has been proposed to have ubiquitin ligase activity, no Smc5/6-dependent ubiquitylation target has been described to date. Here, we review the function of the two RING domains of the Smc5/6 complex in the broader context of SMC complexes as global chromosome organizers of the genome.Work in the J.T.-R. lab is supported by grant and PGC2018-097796-B-I00 from Ministerio de Ciencia, Innovación y Universidades and grant 2017-SGR-569 from AGAUR-Generalitat de Catalunya. R.S.-S. is a recipient of an FPU16/07021 fellowship from Ministerio de Ciencia, Innovación y Universidades. The IRBLLEIDA Institute is part of CERCA Programme/Generalitat de CatalunyaPortland Press2021202120202021info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://doi.org/10.1042/BST20200389http://hdl.handle.net/10459.1/70771http://hdl.handle.net/10459.1/70771reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)Inglésinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-097796-B-I00Versió postprint del document publicat a: https://doi.org/10.1042/BST20200389Biochemical Society Transactions, 2020, vol. 48, num. 5, p. 2159-2171(c) Solé-Soler, Roger et al., 2020info:eu-repo/semantics/openAccessoai:recercat.cat:10459.1/707712026-05-29T05:05:01Z
dc.title.none.fl_str_mv Smc5/6, an atypical SMC complex with two RING-type subunits
title Smc5/6, an atypical SMC complex with two RING-type subunits
spellingShingle Smc5/6, an atypical SMC complex with two RING-type subunits
Solé-Soler, Roger
Chromosomes
E3 ligases
SMC complex
Smc5/6
SUMO
Ubiquitin
title_short Smc5/6, an atypical SMC complex with two RING-type subunits
title_full Smc5/6, an atypical SMC complex with two RING-type subunits
title_fullStr Smc5/6, an atypical SMC complex with two RING-type subunits
title_full_unstemmed Smc5/6, an atypical SMC complex with two RING-type subunits
title_sort Smc5/6, an atypical SMC complex with two RING-type subunits
dc.creator.none.fl_str_mv Solé-Soler, Roger
Torres Rosell, Jordi
author Solé-Soler, Roger
author_facet Solé-Soler, Roger
Torres Rosell, Jordi
author_role author
author2 Torres Rosell, Jordi
author2_role author
dc.subject.none.fl_str_mv Chromosomes
E3 ligases
SMC complex
Smc5/6
SUMO
Ubiquitin
topic Chromosomes
E3 ligases
SMC complex
Smc5/6
SUMO
Ubiquitin
description Smc5/6, an atypical SMC complex with two RING-type subunits Roger Solé-Soler ; Jordi Torres-Rosell Crossmark: Check for Updates Biochem Soc Trans (2020) 48 (5): 2159-2171. https://doi.org/10.1042/BST20200389 Article history Share Icon Share Cite Icon Cite Get Permissions The Smc5/6 complex plays essential roles in chromosome segregation and repair, by promoting disjunction of sister chromatids. The core of the complex is constituted by an heterodimer of Structural Maintenance of Chromosomes (SMC) proteins that use ATP hydrolysis to dynamically associate with and organize chromosomes. In addition, the Smc5/6 complex contains six non-SMC subunits. Remarkably, and differently to other SMC complexes, the Nse1 and Nse2 subunits contain RING-type domains typically found in E3 ligases, pointing to the capacity to regulate other proteins and complexes through ubiquitin-like modifiers. Nse2 codes for a C-terminal SP-RING domain with SUMO ligase activity, assisting Smc5/6 functions in chromosome segregation through sumoylation of several chromosome-associated proteins. Nse1 codes for a C-terminal NH-RING domain and, although it has been proposed to have ubiquitin ligase activity, no Smc5/6-dependent ubiquitylation target has been described to date. Here, we review the function of the two RING domains of the Smc5/6 complex in the broader context of SMC complexes as global chromosome organizers of the genome.
publishDate 2020
dc.date.none.fl_str_mv 2020
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://doi.org/10.1042/BST20200389
http://hdl.handle.net/10459.1/70771
http://hdl.handle.net/10459.1/70771
url https://doi.org/10.1042/BST20200389
http://hdl.handle.net/10459.1/70771
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-097796-B-I00
Versió postprint del document publicat a: https://doi.org/10.1042/BST20200389
Biochemical Society Transactions, 2020, vol. 48, num. 5, p. 2159-2171
dc.rights.none.fl_str_mv (c) Solé-Soler, Roger et al., 2020
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Solé-Soler, Roger et al., 2020
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Portland Press
publisher.none.fl_str_mv Portland Press
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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