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JXB Advance Access originally published online on November 15, 2004
Journal of Experimental Botany 2005 56(411):357-363; doi:10.1093/jxb/eri021
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Journal of Experimental Botany, Vol. 56, No. 411, © Society for Experimental Biology 2004; all rights reserved

RESEARCH PAPER

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

Peter J. Nixon1,*, Myles Barker1, Marko Boehm1, Remco de Vries1 and Josef Komenda2,3

1Wolfson Laboratories, Department of Biological Sciences, Imperial College London, S. Kensington campus, London SW7 2AZ, UK
2Laboratory of Photosynthesis, Institute of Microbiology, Academy of Sciences, Trebon, Czech Republic
3Institute of Physical Biology, University of South Bohemia, Zamek 136, Nove Hrady, Czech Republic

* To whom correspondence should be addressed. Fax: +44 (0) 20 7594 5267. E-mail: p.nixon{at}imperial.ac.uk

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.

Key words: Cyanobacteria, DegP/HtrA proteases, FtsH proteases, light stress, photoinhibition


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