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Characterization of Protein Radicals in Arabidopsis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F19%3A73598027" target="_blank" >RIV/61989592:15310/19:73598027 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.frontiersin.org/articles/10.3389/fphys.2019.00958/full" target="_blank" >https://www.frontiersin.org/articles/10.3389/fphys.2019.00958/full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3389/fphys.2019.00958" target="_blank" >10.3389/fphys.2019.00958</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Characterization of Protein Radicals in Arabidopsis

  • Original language description

    Oxidative modification of proteins in photosystem II (PSII) exposed to high light has been studied for a few decades, but the characterization of protein radicals formed by protein oxidation is largely unknown. Protein oxidation is induced by the direct reaction of proteins with reactive oxygen species known to form highly reactive protein radicals comprising carbon-centered (alkyl) and oxygen-centered (peroxyl and alkoxyl) radicals. In this study, protein radicals were monitored in Arabidopsis exposed to high light by immuno-spin trapping technique based on the detection of 5,5-dimethyl-1-pyrroline N-oxide (DMPO) nitrone adducts using the anti-DMPO antibody. Protein radicals were imaged in Arabidopsis leaves and chloroplasts by confocal laser scanning microscopy using fluorescein conjugated with the anti-DMPO antibody. Characterization of protein radicals by standard blotting techniques using PSII protein specific antibodies shows that protein radicals are formed on D1, D2, CP43, CP47, and Lhcb3 proteins. Protein oxidation reflected by the appearance/disappearance of the protein bands reveals that formation of protein radicals was associated with protein fragmentation (cleavage of the D1 peptide bonds) and aggregation (cross-linking with another PSII subunits). Characterization of protein radical formation is important for better understating of the mechanism of oxidative modification of PSII proteins under high light.

  • 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

    10610 - Biophysics

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Plants as a tool for sustainable global development</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Frontiers in Physiology

  • ISSN

    1664-042X

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    AUG

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    10

  • Pages from-to

    "958-1"-"958-10"

  • UT code for WoS article

    000480560400001

  • EID of the result in the Scopus database

    2-s2.0-85070554950