H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity

Background: Polycomb group complexes PRC1 and PRC2 repress gene expression at the chromatin level in eukaryotes. The classic recruitment model of Polycomb group complexes in which PRC2-mediated H3K27 trimethylation recruits PRC1 for H2A monoubiquitination was recently challenged by data showing that...

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Autores: Zhou, Yue, Romero-Campero, Francisco J., Gómez-Zambrano, Ángeles, Turck, Franzisca, Calonje, Myriam
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2017
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/150013
Acceso en línea:http://hdl.handle.net/10261/150013
Access Level:acceso abierto
Palabra clave:Polycomb group repression mechanism
PRC1
PRC2
H2AK121ub
H3K27me3
Arabidopsis thaliana
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spelling H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activityZhou, YueRomero-Campero, Francisco J.Gómez-Zambrano, ÁngelesTurck, FranziscaCalonje, MyriamPolycomb group repression mechanismPRC1PRC2H2AK121ubH3K27me3Arabidopsis thalianaBackground: Polycomb group complexes PRC1 and PRC2 repress gene expression at the chromatin level in eukaryotes. The classic recruitment model of Polycomb group complexes in which PRC2-mediated H3K27 trimethylation recruits PRC1 for H2A monoubiquitination was recently challenged by data showing that PRC1 activity can also recruit PRC2. However, the prevalence of these two mechanisms is unknown, especially in plants as H2AK121ub marks were examined at only a handful of Polycomb group targets. Results: By using genome-wide analyses, we show that H2AK121ub marks are surprisingly widespread in Arabidopsis thaliana, often co-localizing with H3K27me3 but also occupying a set of transcriptionally active genes devoid of H3K27me3. Furthermore, by profiling H2AK121ub and H3K27me3 marks in atbmi1a/b/c, clf/swn, and lhp1 mutants we found that PRC2 activity is not required for H2AK121ub marking at most genes. In contrast, loss of AtBMI1 function impacts the incorporation of H3K27me3 marks at most Polycomb group targets. Conclusions: Our findings show the relationship between H2AK121ub and H3K27me3 marks across the A. thaliana genome and unveil that ubiquitination by PRC1 is largely independent of PRC2 activity in plants, while the inverse is true for H3K27 trimethylation.Peer reviewedBioMed CentralConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201720172017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/150013reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1186/s13059-017-1197-zSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1500132026-05-22T06:33:51Z
dc.title.none.fl_str_mv H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
title H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
spellingShingle H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
Zhou, Yue
Polycomb group repression mechanism
PRC1
PRC2
H2AK121ub
H3K27me3
Arabidopsis thaliana
title_short H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
title_full H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
title_fullStr H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
title_full_unstemmed H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
title_sort H2A monoubiquitination in Arabidopsis thaliana is generally independent of LHP1 and PRC2 activity
dc.creator.none.fl_str_mv Zhou, Yue
Romero-Campero, Francisco J.
Gómez-Zambrano, Ángeles
Turck, Franzisca
Calonje, Myriam
author Zhou, Yue
author_facet Zhou, Yue
Romero-Campero, Francisco J.
Gómez-Zambrano, Ángeles
Turck, Franzisca
Calonje, Myriam
author_role author
author2 Romero-Campero, Francisco J.
Gómez-Zambrano, Ángeles
Turck, Franzisca
Calonje, Myriam
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Polycomb group repression mechanism
PRC1
PRC2
H2AK121ub
H3K27me3
Arabidopsis thaliana
topic Polycomb group repression mechanism
PRC1
PRC2
H2AK121ub
H3K27me3
Arabidopsis thaliana
description Background: Polycomb group complexes PRC1 and PRC2 repress gene expression at the chromatin level in eukaryotes. The classic recruitment model of Polycomb group complexes in which PRC2-mediated H3K27 trimethylation recruits PRC1 for H2A monoubiquitination was recently challenged by data showing that PRC1 activity can also recruit PRC2. However, the prevalence of these two mechanisms is unknown, especially in plants as H2AK121ub marks were examined at only a handful of Polycomb group targets. Results: By using genome-wide analyses, we show that H2AK121ub marks are surprisingly widespread in Arabidopsis thaliana, often co-localizing with H3K27me3 but also occupying a set of transcriptionally active genes devoid of H3K27me3. Furthermore, by profiling H2AK121ub and H3K27me3 marks in atbmi1a/b/c, clf/swn, and lhp1 mutants we found that PRC2 activity is not required for H2AK121ub marking at most genes. In contrast, loss of AtBMI1 function impacts the incorporation of H3K27me3 marks at most Polycomb group targets. Conclusions: Our findings show the relationship between H2AK121ub and H3K27me3 marks across the A. thaliana genome and unveil that ubiquitination by PRC1 is largely independent of PRC2 activity in plants, while the inverse is true for H3K27 trimethylation.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/150013
url http://hdl.handle.net/10261/150013
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1186/s13059-017-1197-z
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv BioMed Central
publisher.none.fl_str_mv BioMed Central
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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