Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2

Autores
Baidanoff, Fernando Martín; Trebucq, Laura Lucía; Plano, Santiago Andrés; Eaton, Phillip; Golombek, Diego Andres; Chiesa, Juan José
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Plano, Santiago Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Eaton, Phillip. Queen Mary University of London; Reino Unido
Fil: Golombek, Diego Andres. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
CIRCADIAN CLOCK
PER2
REDOX
S-NITROSATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/206032
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2Baidanoff, Fernando MartínTrebucq, Laura LucíaPlano, Santiago AndrésEaton, PhillipGolombek, Diego AndresChiesa, Juan JoséCIRCADIAN CLOCKPER2REDOXS-NITROSATIONhttps://purl.org/becyt/ford/3.5https://purl.org/becyt/ford/3The 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.Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Plano, Santiago Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; ArgentinaFil: Eaton, Phillip. Queen Mary University of London; Reino UnidoFil: Golombek, Diego Andres. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMDPI2022-07info: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/11336/206032Baidanoff, Fernando Martín; Trebucq, Laura Lucía; Plano, Santiago Andrés; Eaton, Phillip; Golombek, Diego Andres; et al.; Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2; MDPI; Biomolecules; 12; 7; 7-2022; 1-102218-273XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/12/7/892info:eu-repo/semantics/altIdentifier/doi/10.3390/biom12070892info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:49:44Zoai:ri.conicet.gov.ar:11336/206032instacron: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:34982025-10-15 14:49:44.417CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
title Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
spellingShingle Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
Baidanoff, Fernando Martín
CIRCADIAN CLOCK
PER2
REDOX
S-NITROSATION
title_short Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
title_full Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
title_fullStr Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
title_full_unstemmed Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
title_sort Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
dc.creator.none.fl_str_mv Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego Andres
Chiesa, Juan José
author Baidanoff, Fernando Martín
author_facet Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego Andres
Chiesa, Juan José
author_role author
author2 Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego Andres
Chiesa, Juan José
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv CIRCADIAN CLOCK
PER2
REDOX
S-NITROSATION
topic CIRCADIAN CLOCK
PER2
REDOX
S-NITROSATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.5
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv 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.
Fil: Baidanoff, Fernando Martín. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Trebucq, Laura Lucía. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Plano, Santiago Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Eaton, Phillip. Queen Mary University of London; Reino Unido
Fil: Golombek, Diego Andres. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Chiesa, Juan José. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description 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.
publishDate 2022
dc.date.none.fl_str_mv 2022-07
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/11336/206032
Baidanoff, Fernando Martín; Trebucq, Laura Lucía; Plano, Santiago Andrés; Eaton, Phillip; Golombek, Diego Andres; et al.; Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2; MDPI; Biomolecules; 12; 7; 7-2022; 1-10
2218-273X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/206032
identifier_str_mv Baidanoff, Fernando Martín; Trebucq, Laura Lucía; Plano, Santiago Andrés; Eaton, Phillip; Golombek, Diego Andres; et al.; Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2; MDPI; Biomolecules; 12; 7; 7-2022; 1-10
2218-273X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/12/7/892
info:eu-repo/semantics/altIdentifier/doi/10.3390/biom12070892
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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
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score 13.22299

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