Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
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 pro...
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| Published in | Biomolecules (Basel, Switzerland) Vol. 12; no. 7; p. 892 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Basel
MDPI AG
25.06.2022
MDPI |
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| Online Access | Get full text |
| ISSN | 2218-273X 2218-273X |
| DOI | 10.3390/biom12070892 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Author | Golombek, Diego Andrés Baidanoff, Fernando Martin Chiesa, Juan José Plano, Santiago Andrés Eaton, Phillip Trebucq, Laura Lucía |
| AuthorAffiliation | 2 Institute for Biomedical Research (BIOMED), Catholic University of Argentina/CONICET, Buenos Aires C1107CABA, Argentina; splano@gmail.com 3 William Harvey Research Institute, Queen Mary University of London, London EC1M 6BQ, UK; p.eaton@qmul.ac.uk 1 Laboratorio de Cronobiología, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes/CONICET, Bernal B1876BXD, Argentina; fbaidanoff@gmail.com (F.M.B.); laura.trebucq@gmail.com (L.L.T.); dgolombek@gmail.com (D.A.G.) |
| AuthorAffiliation_xml | – name: 2 Institute for Biomedical Research (BIOMED), Catholic University of Argentina/CONICET, Buenos Aires C1107CABA, Argentina; splano@gmail.com – name: 3 William Harvey Research Institute, Queen Mary University of London, London EC1M 6BQ, UK; p.eaton@qmul.ac.uk – name: 1 Laboratorio de Cronobiología, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes/CONICET, Bernal B1876BXD, Argentina; fbaidanoff@gmail.com (F.M.B.); laura.trebucq@gmail.com (L.L.T.); dgolombek@gmail.com (D.A.G.) |
| Author_xml | – sequence: 1 givenname: Fernando Martin surname: Baidanoff fullname: Baidanoff, Fernando Martin – sequence: 2 givenname: Laura Lucía surname: Trebucq fullname: Trebucq, Laura Lucía – sequence: 3 givenname: Santiago Andrés surname: Plano fullname: Plano, Santiago Andrés – sequence: 4 givenname: Phillip surname: Eaton fullname: Eaton, Phillip – sequence: 5 givenname: Diego Andrés orcidid: 0000-0002-6291-5586 surname: Golombek fullname: Golombek, Diego Andrés – sequence: 6 givenname: Juan José orcidid: 0000-0003-1870-5714 surname: Chiesa fullname: Chiesa, Juan José |
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| CitedBy_id | crossref_primary_10_3390_biom13091281 crossref_primary_10_1007_s12010_023_04330_2 crossref_primary_10_3389_fchem_2024_1436322 |
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| SubjectTerms | 2-Mercaptoethanol circadian clock Circadian rhythm Circadian rhythms Cysteine Dimerization Hydrogen peroxide Kinases Molecular weight Nitrosation Oligomerization Oxidation PER2 Period 2 protein Polyethylene glycol Post-translation Proteins redox Redox reactions S-nitrosation Thiols Translation |
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| Title | Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2 |
| URI | https://www.proquest.com/docview/2693908211 https://www.proquest.com/docview/2695293631 https://pubmed.ncbi.nlm.nih.gov/PMC9313148 https://doaj.org/article/66a78104f3074c83b02c9281521923c7 |
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