Cysteine oxidation promotes dimerization/oligomerization of circadian protein period

Autores
Baidanoff, Fernando Martín; Trebucq, Laura Lucía; Plano, Santiago Andrés; Eaton, Phillip; Golombek, Diego A.; Chiesa, Juan José
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Baidanoff, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Trebucq, Laura Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Plano, Santiago Andrés. Pontificia Universidad Católica Argentina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Eaton, Phillip. Queen Mary University of London. William Harvey Research Institute; Reino Unido
Fil: Golombek, Diego Andrés. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Golombek, Diego Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Chiesa, Juan José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: The molecular circadian clock is based on a transcriptional/translational feedback loop in which the stability and half-life of circadian proteins is of importance. Cysteine residues of proteins are subject to several redox reactions leading to S-thiolation and disulfide bond formation, altering protein stability and function. In this work, the ability of the circadian protein period 2 (PER2) to undergo oxidation of cysteine thiols was investigated in HEK-293T cells. PER2 includes accessible cysteines susceptible to oxidation by nitroso cysteine (CysNO), altering its stability by decreasing its monomer form and subsequently increasing PER2 homodimers and multimers. These changes were reversed by treatment with 2-mercaptoethanol and partially mimicked by hydrogen peroxide. These results suggest that cysteine oxidation can prompt PER2 homodimer and multimer formation in vitro, likely by S-nitrosation and disulphide bond formation. These kinds of post-translational modifications of PER2 could be part of the redox regulation of the molecular circadian clock.
Fuente
Biomolecules Vol.12, No.7, 2022
Materia
REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/15390
Acceder
id RIUCA_07812904f87f3b090adac9f7dd6d4d15
oai_identifier_str oai:ucacris:123456789/15390
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Cysteine oxidation promotes dimerization/oligomerization of circadian protein periodBaidanoff, Fernando MartínTrebucq, Laura LucíaPlano, Santiago AndrésEaton, PhillipGolombek, Diego A.Chiesa, Juan JoséREDOXRELOJ CIRCADIANOS-NITROSACIÓNPER2Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; ArgentinaFil: Baidanoff, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; ArgentinaFil: Trebucq, Laura Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Plano, Santiago Andrés. Pontificia Universidad Católica Argentina. Instituto de Investigaciones Biomédicas; ArgentinaFil: Eaton, Phillip. Queen Mary University of London. William Harvey Research Institute; Reino UnidoFil: Golombek, Diego Andrés. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; ArgentinaFil: Golombek, Diego Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; ArgentinaFil: Chiesa, Juan José. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAbstract: The molecular circadian clock is based on a transcriptional/translational feedback loop in which the stability and half-life of circadian proteins is of importance. Cysteine residues of proteins are subject to several redox reactions leading to S-thiolation and disulfide bond formation, altering protein stability and function. In this work, the ability of the circadian protein period 2 (PER2) to undergo oxidation of cysteine thiols was investigated in HEK-293T cells. PER2 includes accessible cysteines susceptible to oxidation by nitroso cysteine (CysNO), altering its stability by decreasing its monomer form and subsequently increasing PER2 homodimers and multimers. These changes were reversed by treatment with 2-mercaptoethanol and partially mimicked by hydrogen peroxide. These results suggest that cysteine oxidation can prompt PER2 homodimer and multimer formation in vitro, likely by S-nitrosation and disulphide bond formation. These kinds of post-translational modifications of PER2 could be part of the redox regulation of the molecular circadian clock.Multidisciplinary Digital Publishing Institute2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/153902218-273X (oniline)10.3390/biom1207089235883448Baidanoff, F. M. et al. Cysteine oxidation promotes dimerization/oligomerization of circadian protein period [en línea]. Biomolecules. 2022, 12 (7). doi: 10.3390/biom12070892. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15390Biomolecules Vol.12, No.7, 2022reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:58:57Zoai:ucacris:123456789/15390instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:58:57.838Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
title Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
spellingShingle Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
Baidanoff, Fernando Martín
REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
title_short Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
title_full Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
title_fullStr Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
title_full_unstemmed Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
title_sort Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
dc.creator.none.fl_str_mv Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
author Baidanoff, Fernando Martín
author_facet Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
author_role author
author2 Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
topic REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
dc.description.none.fl_txt_mv Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Baidanoff, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Trebucq, Laura Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Plano, Santiago Andrés. Pontificia Universidad Católica Argentina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Eaton, Phillip. Queen Mary University of London. William Harvey Research Institute; Reino Unido
Fil: Golombek, Diego Andrés. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Golombek, Diego Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
Fil: Chiesa, Juan José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: The molecular circadian clock is based on a transcriptional/translational feedback loop in which the stability and half-life of circadian proteins is of importance. Cysteine residues of proteins are subject to several redox reactions leading to S-thiolation and disulfide bond formation, altering protein stability and function. In this work, the ability of the circadian protein period 2 (PER2) to undergo oxidation of cysteine thiols was investigated in HEK-293T cells. PER2 includes accessible cysteines susceptible to oxidation by nitroso cysteine (CysNO), altering its stability by decreasing its monomer form and subsequently increasing PER2 homodimers and multimers. These changes were reversed by treatment with 2-mercaptoethanol and partially mimicked by hydrogen peroxide. These results suggest that cysteine oxidation can prompt PER2 homodimer and multimer formation in vitro, likely by S-nitrosation and disulphide bond formation. These kinds of post-translational modifications of PER2 could be part of the redox regulation of the molecular circadian clock.
description Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Cronobiología; Argentina
publishDate 2022
dc.date.none.fl_str_mv 2022
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 https://repositorio.uca.edu.ar/handle/123456789/15390
2218-273X (oniline)
10.3390/biom12070892
35883448
Baidanoff, F. M. et al. Cysteine oxidation promotes dimerization/oligomerization of circadian protein period [en línea]. Biomolecules. 2022, 12 (7). doi: 10.3390/biom12070892. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15390
url https://repositorio.uca.edu.ar/handle/123456789/15390
identifier_str_mv 2218-273X (oniline)
10.3390/biom12070892
35883448
Baidanoff, F. M. et al. Cysteine oxidation promotes dimerization/oligomerization of circadian protein period [en línea]. Biomolecules. 2022, 12 (7). doi: 10.3390/biom12070892. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/15390
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv Biomolecules Vol.12, No.7, 2022
reponame:Repositorio Institucional (UCA)
instname:Pontificia Universidad Católica Argentina
reponame_str Repositorio Institucional (UCA)
collection Repositorio Institucional (UCA)
instname_str Pontificia Universidad Católica Argentina
repository.name.fl_str_mv Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina
repository.mail.fl_str_mv claudia_fernandez@uca.edu.ar
_version_ 1836638365890379776
score 13.070432

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