p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage

Autores
Gironella, Meritxell; Malicet, Cedric; Cano, Carla; Sandi, Maria Jose; Hamidi, Tewfic; Neme Tauil, Ricardo Martin; Baston, Mariela; Valacco, Maria Pia; Moreno, Silvia Margarita; Lopez, Frederic; Neira, Jose Luis; Dagorn, Juan Charles; Iovanna, Juan Lucio
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The stress protein p8 is a small, highly basic, unfolded, and multifunctional protein. We have previously shown that most of its functions are exerted through interactions with other proteins, whose activities are thereby enhanced or repressed. In this work we describe another example of such mechanism, by which p8 binds and negatively regulates MSL1, a histone acetyl transferase (HAT)-associated protein, which in turn binds the DNA-damage-associated 53BP1 protein to facilitate DNA repair following DNA gamma-irradiation. Contrary to the HAT-associated activity, MSL1-dependent DNA-repair activity is almost completely dependent on 53BP1 expression. The picture that has emerged from our findings is that 53BP1 could be a scaffold that gets the HAT MSL1-dependent DNA-repair activity to the sites of DNA damage. Finally, we also found that, although p8 expression is transiently activated after gamma-irradiation, it is eventually submitted to sustained down-regulation, presumably to allow development of MSL1-associated DNA-repair activity. We conclude that interaction of MSL1 with 53BP1 brings MSL1-dependent HAT activity to the vicinity of damaged DNA. MSL1-dependent HAT activity, which is negatively regulated by the stress protein p8, induces chromatin remodeling and relaxation allowing access to DNA of the repair machinery
Fil: Gironella, Meritxell. Inserm; Francia. Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas; España
Fil: Malicet, Cedric. Inserm; Francia
Fil: Cano, Carla. Inserm; Francia
Fil: Sandi, Maria Jose. Inserm; Francia
Fil: Hamidi, Tewfic. Inserm; Francia
Fil: Neme Tauil, Ricardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Baston, Mariela. Inserm; Francia
Fil: Valacco, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Lopez, Frederic. Inserm; Francia
Fil: Neira, Jose Luis. Universidad Miguel Hernandez; España
Fil: Dagorn, Juan Charles. Inserm; Francia
Fil: Iovanna, Juan Lucio. Inserm; Francia
Materia
P8
Msl1
Dna Repair
Hat
Yeast Two-Hybrid Screening
Tp53bp1
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/28429

id CONICETDig_1951c9df9a752f61594ef3765c443cc3
oai_identifier_str oai:ri.conicet.gov.ar:11336/28429
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damageGironella, MeritxellMalicet, CedricCano, CarlaSandi, Maria JoseHamidi, TewficNeme Tauil, Ricardo MartinBaston, MarielaValacco, Maria PiaMoreno, Silvia MargaritaLopez, FredericNeira, Jose LuisDagorn, Juan CharlesIovanna, Juan LucioP8Msl1Dna RepairHatYeast Two-Hybrid ScreeningTp53bp1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The stress protein p8 is a small, highly basic, unfolded, and multifunctional protein. We have previously shown that most of its functions are exerted through interactions with other proteins, whose activities are thereby enhanced or repressed. In this work we describe another example of such mechanism, by which p8 binds and negatively regulates MSL1, a histone acetyl transferase (HAT)-associated protein, which in turn binds the DNA-damage-associated 53BP1 protein to facilitate DNA repair following DNA gamma-irradiation. Contrary to the HAT-associated activity, MSL1-dependent DNA-repair activity is almost completely dependent on 53BP1 expression. The picture that has emerged from our findings is that 53BP1 could be a scaffold that gets the HAT MSL1-dependent DNA-repair activity to the sites of DNA damage. Finally, we also found that, although p8 expression is transiently activated after gamma-irradiation, it is eventually submitted to sustained down-regulation, presumably to allow development of MSL1-associated DNA-repair activity. We conclude that interaction of MSL1 with 53BP1 brings MSL1-dependent HAT activity to the vicinity of damaged DNA. MSL1-dependent HAT activity, which is negatively regulated by the stress protein p8, induces chromatin remodeling and relaxation allowing access to DNA of the repair machineryFil: Gironella, Meritxell. Inserm; Francia. Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas; EspañaFil: Malicet, Cedric. Inserm; FranciaFil: Cano, Carla. Inserm; FranciaFil: Sandi, Maria Jose. Inserm; FranciaFil: Hamidi, Tewfic. Inserm; FranciaFil: Neme Tauil, Ricardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Baston, Mariela. Inserm; FranciaFil: Valacco, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Lopez, Frederic. Inserm; FranciaFil: Neira, Jose Luis. Universidad Miguel Hernandez; EspañaFil: Dagorn, Juan Charles. Inserm; FranciaFil: Iovanna, Juan Lucio. Inserm; FranciaWiley2009-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/28429Gironella, Meritxell; Malicet, Cedric; Cano, Carla; Sandi, Maria Jose; Hamidi, Tewfic; et al.; p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage; Wiley; Journal of Cellular Physiology; 221; 3; 12-2009; 594-6020021-95411097-4652CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jcp.21889info:eu-repo/semantics/altIdentifier/doi/10.1002/jcp.21889info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:03:13Zoai:ri.conicet.gov.ar:11336/28429instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:03:14.119CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
title p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
spellingShingle p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
Gironella, Meritxell
P8
Msl1
Dna Repair
Hat
Yeast Two-Hybrid Screening
Tp53bp1
title_short p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
title_full p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
title_fullStr p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
title_full_unstemmed p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
title_sort p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
dc.creator.none.fl_str_mv Gironella, Meritxell
Malicet, Cedric
Cano, Carla
Sandi, Maria Jose
Hamidi, Tewfic
Neme Tauil, Ricardo Martin
Baston, Mariela
Valacco, Maria Pia
Moreno, Silvia Margarita
Lopez, Frederic
Neira, Jose Luis
Dagorn, Juan Charles
Iovanna, Juan Lucio
author Gironella, Meritxell
author_facet Gironella, Meritxell
Malicet, Cedric
Cano, Carla
Sandi, Maria Jose
Hamidi, Tewfic
Neme Tauil, Ricardo Martin
Baston, Mariela
Valacco, Maria Pia
Moreno, Silvia Margarita
Lopez, Frederic
Neira, Jose Luis
Dagorn, Juan Charles
Iovanna, Juan Lucio
author_role author
author2 Malicet, Cedric
Cano, Carla
Sandi, Maria Jose
Hamidi, Tewfic
Neme Tauil, Ricardo Martin
Baston, Mariela
Valacco, Maria Pia
Moreno, Silvia Margarita
Lopez, Frederic
Neira, Jose Luis
Dagorn, Juan Charles
Iovanna, Juan Lucio
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv P8
Msl1
Dna Repair
Hat
Yeast Two-Hybrid Screening
Tp53bp1
topic P8
Msl1
Dna Repair
Hat
Yeast Two-Hybrid Screening
Tp53bp1
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The stress protein p8 is a small, highly basic, unfolded, and multifunctional protein. We have previously shown that most of its functions are exerted through interactions with other proteins, whose activities are thereby enhanced or repressed. In this work we describe another example of such mechanism, by which p8 binds and negatively regulates MSL1, a histone acetyl transferase (HAT)-associated protein, which in turn binds the DNA-damage-associated 53BP1 protein to facilitate DNA repair following DNA gamma-irradiation. Contrary to the HAT-associated activity, MSL1-dependent DNA-repair activity is almost completely dependent on 53BP1 expression. The picture that has emerged from our findings is that 53BP1 could be a scaffold that gets the HAT MSL1-dependent DNA-repair activity to the sites of DNA damage. Finally, we also found that, although p8 expression is transiently activated after gamma-irradiation, it is eventually submitted to sustained down-regulation, presumably to allow development of MSL1-associated DNA-repair activity. We conclude that interaction of MSL1 with 53BP1 brings MSL1-dependent HAT activity to the vicinity of damaged DNA. MSL1-dependent HAT activity, which is negatively regulated by the stress protein p8, induces chromatin remodeling and relaxation allowing access to DNA of the repair machinery
Fil: Gironella, Meritxell. Inserm; Francia. Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas; España
Fil: Malicet, Cedric. Inserm; Francia
Fil: Cano, Carla. Inserm; Francia
Fil: Sandi, Maria Jose. Inserm; Francia
Fil: Hamidi, Tewfic. Inserm; Francia
Fil: Neme Tauil, Ricardo Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Baston, Mariela. Inserm; Francia
Fil: Valacco, Maria Pia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Lopez, Frederic. Inserm; Francia
Fil: Neira, Jose Luis. Universidad Miguel Hernandez; España
Fil: Dagorn, Juan Charles. Inserm; Francia
Fil: Iovanna, Juan Lucio. Inserm; Francia
description The stress protein p8 is a small, highly basic, unfolded, and multifunctional protein. We have previously shown that most of its functions are exerted through interactions with other proteins, whose activities are thereby enhanced or repressed. In this work we describe another example of such mechanism, by which p8 binds and negatively regulates MSL1, a histone acetyl transferase (HAT)-associated protein, which in turn binds the DNA-damage-associated 53BP1 protein to facilitate DNA repair following DNA gamma-irradiation. Contrary to the HAT-associated activity, MSL1-dependent DNA-repair activity is almost completely dependent on 53BP1 expression. The picture that has emerged from our findings is that 53BP1 could be a scaffold that gets the HAT MSL1-dependent DNA-repair activity to the sites of DNA damage. Finally, we also found that, although p8 expression is transiently activated after gamma-irradiation, it is eventually submitted to sustained down-regulation, presumably to allow development of MSL1-associated DNA-repair activity. We conclude that interaction of MSL1 with 53BP1 brings MSL1-dependent HAT activity to the vicinity of damaged DNA. MSL1-dependent HAT activity, which is negatively regulated by the stress protein p8, induces chromatin remodeling and relaxation allowing access to DNA of the repair machinery
publishDate 2009
dc.date.none.fl_str_mv 2009-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/28429
Gironella, Meritxell; Malicet, Cedric; Cano, Carla; Sandi, Maria Jose; Hamidi, Tewfic; et al.; p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage; Wiley; Journal of Cellular Physiology; 221; 3; 12-2009; 594-602
0021-9541
1097-4652
CONICET Digital
CONICET
url http://hdl.handle.net/11336/28429
identifier_str_mv Gironella, Meritxell; Malicet, Cedric; Cano, Carla; Sandi, Maria Jose; Hamidi, Tewfic; et al.; p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage; Wiley; Journal of Cellular Physiology; 221; 3; 12-2009; 594-602
0021-9541
1097-4652
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jcp.21889
info:eu-repo/semantics/altIdentifier/doi/10.1002/jcp.21889
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781260294258688
score 13.199325