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On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5)

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00559327" target="_blank" >RIV/61388971:_____/20:00559327 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/19:00522047

  • Result on the web

    <a href="https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15160" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.15160</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1111/febs.15160" target="_blank" >10.1111/febs.15160</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5)

  • Original language description

    It is now accepted that reactive oxygen species (ROS) are not only dangerous oxidative agents but also chemical mediators of the redox cell signaling and innate immune response. A central role in ROS-controlled production is played by the NADPH oxidases (NOXs), a group of seven membrane-bound enzymes (NOX1-5 and DUOX1-2) whose unique function is to produce ROS. Here, we describe the regulation of NOX5, a widespread family member present in cyanobacteria, protists, plants, fungi, and the animal kingdom. We show that the calmodulin-like regulatory EF-domain of NOX5 is partially unfolded and detached from the rest of the protein in the absence of calcium. In the presence of calcium, the C-terminal lobe of the EF-domain acquires an ordered and more compact structure that enables its binding to the enzyme dehydrogenase (DH) domain. Our spectroscopic and mutagenesis studies further identified a set of conserved aspartate residues in the DH domain that are essential for NOX5 activation. Altogether, our work shows that calcium induces an unfolded-to-folded transition of the EF-domain that promotes direct interaction with a conserved regulatory region, resulting in NOX5 activation.

  • 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

    10606 - Microbiology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    FEBS Journal

  • ISSN

    1742-464X

  • e-ISSN

    1742-4658

  • Volume of the periodical

    287

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    18

  • Pages from-to

    2486-2503

  • UT code for WoS article

    000503619000001

  • EID of the result in the Scopus database

    2-s2.0-85076814616