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A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo

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UNSPECIFIED. (2002) A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo. JOURNAL OF BIOLOGICAL CHEMISTRY, 277 (3). pp. 2006-2011. ISSN 0021-9258

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Official URL: http://dx.doi.org/10.1074/jbc.M105878200

Abstract

Using a var2-2 mutant of Arabidopsis thaliana, which lacks a homologue of the zinc-metalloprotease, FtsH, we demonstrate that this protease is required for the efficient turnover of the D1 polypeptide of photosystem II and protection against photoinhibition in vivo. We show that var2-2 leaves are much more susceptible to light-induced photosystem II photoinhibition than wild-type leaves. Furthermore, the rate of photosystem II photoinhibition in untreated var2-2 leaves is equivalent to that of var2-2 and wild-type leaves, which have been treated with lincomycin, an inhibitor of the photosystem II repair cycle at the level of D1 synthesis. This is in contrast to untreated wild-type leaves, which show a much slower rate of photosystem II photoinhibition due to an efficient photosystem II repair cycle. The recovery of var2-2 leaves from photosystem II photoinhibition is also impaired relative to wild-type. Using Western blot analysis in the presence of lincomycin we show that the D1 polypeptide remains stable in leaves of the var2-2 mutant under photoinhibitory conditions that lead to D1 degradation in wild-type leaves and that the abundance of DegP2 is not affected by the var2-2 mutation. We conclude, therefore, that the Var2 FtsH homologue is required for the cleavage of the D1 polypeptide in vivo. In addition, we identify a conserved lumenal domain in Var2 that is unique to FtsH homologues from oxygenic phototrophs.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Journal or Publication Title: JOURNAL OF BIOLOGICAL CHEMISTRY
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN: 0021-9258
Date: 18 January 2002
Volume: 277
Number: 3
Number of Pages: 6
Page Range: pp. 2006-2011
Identification Number: 10.1074/jbc.M105878200
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/11305

Data sourced from Thomson Reuters' Web of Knowledge

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