Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation

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Publikace nespadá pod Pedagogickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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EVIC Valentina SOIC Ruzica MOCIBOB Marko KEKEZ Mario HOUSER Josef WIMMEROVÁ Michaela MATKOVIĆ-ČALOGOVIĆ Dubravka GRUIC-SOVULJ Ita KEKEZ Ivana ROKOV-PLAVEC Jasmina

Rok publikování 2023
Druh Článek v odborném periodiku
Časopis / Zdroj FEBS Letters
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14748
Doi http://dx.doi.org/10.1002/1873-3468.14748
Klíčová slova aminoacyl-tRNA synthetase; cysteine reactivity; disulfide bond; hydrogen peroxide; oxidative stress; thermal stability
Popis We have previously identified a unique disulfide bond in the crystal structure of Arabidopsis cytosolic seryl-tRNA synthetase involving cysteines evolutionarily conserved in all green plants. Here, we discovered that both cysteines are important for protein stability, but with opposite effects, and that their microenvironment may promote disulfide bond formation in oxidizing conditions. The crystal structure of the C244S mutant exhibited higher rigidity and an extensive network of noncovalent interactions correlating with its higher thermal stability. The activity of the wild-type showed resistance to oxidation with H2O2, while the activities of cysteine-to-serine mutants were impaired, indicating that the disulfide link may enable the protein to function under oxidative stress conditions which can be beneficial for an efficient plant stress response.
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