A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility

Nucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A-H2B histone chaperone, and recently it has been shown that it can also interact with...

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Autores: Fernández-Rivero, Noelia, Franco, Aitor, Velázquez-Campoy, Adrián, Alonso, Edurne, Muga, Arturo, Prado, Adelina
Formato: artículo
Fecha de publicación:2016
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/139663
Acesso em linha:http://hdl.handle.net/10261/139663
Access Level:acceso abierto
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spelling A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone VersatilityFernández-Rivero, NoeliaFranco, AitorVelázquez-Campoy, AdriánAlonso, EdurneMuga, ArturoPrado, AdelinaNucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A-H2B histone chaperone, and recently it has been shown that it can also interact with H3-H4. However, its interaction with different types of histones has not been quantitatively studied so far. We show here that NP binds H2A-H2B, H3-H4 and linker histones with K d values in the subnanomolar range, forming different complexes. Post-translational modifications of NP regulate exposure of the polyGlu tract at the disordered distal face of the protein and induce an increase in chaperone affinity for all histones. The relative affinity of NP for H2A-H2B and linker histones and the fact that they interact with the distal face of the chaperone could explain their competition for chaperone binding, a relevant process in NP-mediated sperm chromatin remodelling during fertilization. Our data show that NP binds H3-H4 tetramers in a nucleosomal conformation and dimers, transferring them to DNA to form disomes and tetrasomes. This finding might be relevant to elucidate the role of NP in chromatin disassembly and assembly during replication and transcription.Peer ReviewedNature Publishing GroupConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2016201620162016info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/139663reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1396632026-05-22T06:33:51Z
dc.title.none.fl_str_mv A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
title A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
spellingShingle A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
Fernández-Rivero, Noelia
title_short A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
title_full A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
title_fullStr A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
title_full_unstemmed A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
title_sort A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
dc.creator.none.fl_str_mv Fernández-Rivero, Noelia
Franco, Aitor
Velázquez-Campoy, Adrián
Alonso, Edurne
Muga, Arturo
Prado, Adelina
author Fernández-Rivero, Noelia
author_facet Fernández-Rivero, Noelia
Franco, Aitor
Velázquez-Campoy, Adrián
Alonso, Edurne
Muga, Arturo
Prado, Adelina
author_role author
author2 Franco, Aitor
Velázquez-Campoy, Adrián
Alonso, Edurne
Muga, Arturo
Prado, Adelina
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description Nucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A-H2B histone chaperone, and recently it has been shown that it can also interact with H3-H4. However, its interaction with different types of histones has not been quantitatively studied so far. We show here that NP binds H2A-H2B, H3-H4 and linker histones with K d values in the subnanomolar range, forming different complexes. Post-translational modifications of NP regulate exposure of the polyGlu tract at the disordered distal face of the protein and induce an increase in chaperone affinity for all histones. The relative affinity of NP for H2A-H2B and linker histones and the fact that they interact with the distal face of the chaperone could explain their competition for chaperone binding, a relevant process in NP-mediated sperm chromatin remodelling during fertilization. Our data show that NP binds H3-H4 tetramers in a nucleosomal conformation and dimers, transferring them to DNA to form disomes and tetrasomes. This finding might be relevant to elucidate the role of NP in chromatin disassembly and assembly during replication and transcription.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/139663
url http://hdl.handle.net/10261/139663
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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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score 15,811543

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