FtsH-mediated repair of the photosystem II complex in response to light stress

A common feature of light stress in plants, algae, and cyanobacteria is the light-induced damage to the photosystem II complex (PSII), which catalyses the photosynthetic oxidation of water to molecular oxygen. A repair cycle operates to replace damaged subunits within PSII, in particular, the D1 rea...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 56(2005), 411 vom: 27. Jan., Seite 357-63
1. Verfasser: Nixon, Peter J (VerfasserIn)
Weitere Verfasser: Barker, Myles, Boehm, Marko, de Vries, Remco, Komenda, Josef
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Review Arabidopsis Proteins Heat-Shock Proteins Membrane Proteins Periplasmic Proteins Photosystem II Protein Complex Plant Proteins Reactive Oxygen Species mehr... Peptide Hydrolases EC 3.4.- ATP-Dependent Proteases EC 3.4.21.- DegP protease Serine Endopeptidases VAR2 protein, Arabidopsis
Beschreibung
Zusammenfassung:A common feature of light stress in plants, algae, and cyanobacteria is the light-induced damage to the photosystem II complex (PSII), which catalyses the photosynthetic oxidation of water to molecular oxygen. A repair cycle operates to replace damaged subunits within PSII, in particular, the D1 reaction centre polypeptide, by newly synthesized copies. As yet the molecular details of this physiologically important process remain obscure. A key aspect of the process that has attracted much attention is the identity of the protease or proteases involved in D1 degradation. The results are summarized here of recent mutagenesis experiments that were designed to assess the functional importance of the DegP/HtrA and FtsH protease families in the cyanobacterium Synechocystis sp. PCC 6803. Based on these results and the analysis of Arabidopsis mutants, a general model for PSII repair is suggested in which FtsH complexes alone are able to degrade damaged D1
Beschreibung:Date Completed 11.05.2005
Date Revised 15.11.2006
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431