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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F23%3A00133310" target="_blank" >RIV/00216224:14740/23:00133310 - isvavai.cz</a>

  • Result on the web

    <a href="https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14748" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14748</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/1873-3468.14748" target="_blank" >10.1002/1873-3468.14748</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    FEBS Letters

  • ISSN

    0014-5793

  • e-ISSN

    1873-3468

  • Volume of the periodical

    597

  • Issue of the periodical within the volume

    23

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    18

  • Pages from-to

    2975-2992

  • UT code for WoS article

    001083471700001

  • EID of the result in the Scopus database

    2-s2.0-85173774693