All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Accessibility controls selective degradation of photosystem II subunits by FtsH protease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F15%3A00467583" target="_blank" >RIV/61388971:_____/15:00467583 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/15:43889031

  • Result on the web

    <a href="http://dx.doi.org/10.1038/NPLANTS.2015.168" target="_blank" >http://dx.doi.org/10.1038/NPLANTS.2015.168</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/NPLANTS.2015.168" target="_blank" >10.1038/NPLANTS.2015.168</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Accessibility controls selective degradation of photosystem II subunits by FtsH protease

  • Original language description

    The oxygen-evolving photosystem II (PSII) complex located in chloroplasts and cyanobacteria is sensitive to light-induced damage(1) that unless repaired causes reduction in photosynthetic capacity and growth. Although a potential target for crop improvement, the mechanism of PSII repair remains unclear. The D1 reaction center protein is the main target for photodamage(2), with repair involving the selective degradation of the damaged protein by FtsH protease(3). How a single damaged PSII subunit is recognized for replacement is unknown. Here, we have tested the dark stability of PSII subunits in strains of the cyanobacterium Synechocystis PCC 6803 blocked at specific stages of assembly. We have found that when D1, which is normally shielded by the CP43 subunit, becomes exposed in a photochemically active PSII complex lacking CP43, it is selectively degraded by FtsH even in the dark. Removal of the CP47 subunit, which increases accessibility of FtsH to the D2 subunit, induced dark degradation of D2 at a faster rate than that of D1. In contrast, CP47 and CP43 are resistant to degradation in the dark. Our results indicate that protease accessibility induced by PSII disassembly is an important determinant in the selection of the D1 and D2 subunits to be degraded by FtsH.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nature Plants

  • ISSN

    2055-026X

  • e-ISSN

  • Volume of the periodical

    1

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    6

  • Pages from-to

  • UT code for WoS article

    000364419500002

  • EID of the result in the Scopus database

    2-s2.0-84946887779