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Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73584267" target="_blank" >RIV/61989592:15310/17:73584267 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14310/17:00100142

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0006291X17320685" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0006291X17320685</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbrc.2017.10.090" target="_blank" >10.1016/j.bbrc.2017.10.090</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues

  • Original language description

    Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible Snitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO- donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode.

  • 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

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biochemical and Biophysical Research Communication

  • ISSN

    0006-291X

  • e-ISSN

  • Volume of the periodical

    494

  • Issue of the periodical within the volume

    1-2

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    7

  • Pages from-to

    27-33

  • UT code for WoS article

    000416615300006

  • EID of the result in the Scopus database