Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions.
Life Sci Alliance
; 7(5)2024 May.
Article
em En
| MEDLINE
| ID: mdl-38383455
ABSTRACT
Oxidative post-translational modifications of protein thiols are well recognized as a readily occurring alteration of proteins, which can modify their function and thus control cellular processes. The development of techniques enabling the site-specific assessment of protein thiol oxidation on a proteome-wide scale significantly expanded the number of known oxidation-sensitive protein thiols. However, lacking behind are large-scale data on the redox state of proteins during ageing, a physiological process accompanied by increased levels of endogenous oxidants. Here, we present the landscape of protein thiol oxidation in chronologically aged wild-type Saccharomyces cerevisiae in a time-dependent manner. Our data determine early-oxidation targets in key biological processes governing the de novo production of proteins, protein folding, and degradation, and indicate a hierarchy of cellular responses affected by a reversible redox modification. Comparison with existing datasets in yeast, nematode, fruit fly, and mouse reveals the evolutionary conservation of these oxidation targets. To facilitate accessibility, we integrated the cross-species comparison into the newly developed OxiAge Database.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Compostos de Sulfidrila
/
Proteostase
Limite:
Animals
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article