دورية أكاديمية

Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2

التفاصيل البيبلوغرافية
العنوان: Cysteine Oxidation Promotes Dimerization/Oligomerization of Circadian Protein Period 2
المؤلفون: Baidanoff, Fernando Martín, Trebucq, Laura Lucía, Plano, Santiago Andrés, Eaton, Phillip, Golombek, Diego Andres, Chiesa, Juan José
بيانات النشر: MDPI
المجموعة: CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
مصطلحات موضوعية: CIRCADIAN CLOCK, PER2, REDOX, S-NITROSATION, https://purl.org/becyt/ford/3.5Test, https://purl.org/becyt/ford/3Test
الوصف: 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 ...
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
تدمد: 2218-273X
العلاقة: info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/12/7/892Test; http://hdl.handle.net/11336/206032Test; 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; CONICET Digital; CONICET
الإتاحة: https://doi.org/10.3390/biom12070892Test
http://hdl.handle.net/11336/206032Test
حقوق: info:eu-repo/semantics/openAccess ; https://creativecommons.org/licenses/by/2.5/arTest/
رقم الانضمام: edsbas.6B489308
قاعدة البيانات: BASE