Cysteine oxidation promotes dimerization/oligomerization of circadian protein period

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, a...

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Detalles Bibliográficos
Autores principales: Baidanoff, Fernando Martín, Trebucq, Laura Lucía, Plano, Santiago Andrés, Eaton, Phillip, Golombek, Diego A., Chiesa, Juan José
Formato: Artículo
Lenguaje:Inglés
Publicado: Multidisciplinary Digital Publishing Institute 2022
Materias:
REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/15390
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139-123456789-15390
record_format dspace
spelling I33-R139-123456789-153902024-03-21T18:49:30Z Cysteine oxidation promotes dimerization/oligomerization of circadian protein period Baidanoff, Fernando Martín Trebucq, Laura Lucía Plano, Santiago Andrés Eaton, Phillip Golombek, Diego A. Chiesa, Juan José REDOX RELOJ CIRCADIANO S-NITROSACIÓN PER2 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. 2022-11-03T12:11:52Z 2022-11-03T12:11:52Z 2022 Artículo 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 2218-273X (oniline) https://repositorio.uca.edu.ar/handle/123456789/15390 10.3390/biom12070892 35883448 eng Acceso abierto http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf Multidisciplinary Digital Publishing Institute Biomolecules Vol.12, No.7, 2022
institution Universidad Católica Argentina
institution_str I-33
repository_str R-139
collection Repositorio Institucional de la Universidad Católica Argentina (UCA)
language Inglés
topic REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
spellingShingle REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
topic_facet REDOX
RELOJ CIRCADIANO
S-NITROSACIÓN
PER2
description 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.
format Artículo
author Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
author_facet Baidanoff, Fernando Martín
Trebucq, Laura Lucía
Plano, Santiago Andrés
Eaton, Phillip
Golombek, Diego A.
Chiesa, Juan José
author_sort Baidanoff, Fernando Martín
title Cysteine oxidation promotes dimerization/oligomerization of circadian protein period
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
publisher Multidisciplinary Digital Publishing Institute
publishDate 2022
url https://repositorio.uca.edu.ar/handle/123456789/15390
work_keys_str_mv AT baidanofffernandomartin cysteineoxidationpromotesdimerizationoligomerizationofcircadianproteinperiod
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AT planosantiagoandres cysteineoxidationpromotesdimerizationoligomerizationofcircadianproteinperiod
AT eatonphillip cysteineoxidationpromotesdimerizationoligomerizationofcircadianproteinperiod
AT golombekdiegoa cysteineoxidationpromotesdimerizationoligomerizationofcircadianproteinperiod
AT chiesajuanjose cysteineoxidationpromotesdimerizationoligomerizationofcircadianproteinperiod
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