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Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism.

ABSTRACT: Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge. In their reduced form, they constitute very efficient protein disulfide oxidoreductases. In chloroplasts, two types of Trxs (f and m) coexist and play central roles in the regulation of the Calvin cycle and other processes. Here, we identified a class of Trx targets in the inner plastid envelope membrane of chloroplasts that share a CxxC motif approximately 73 aa from their carboxyl-terminal end. Members of this group belong to a superfamily of Rieske iron-sulfur proteins involved in protein translocation and chlorophyll metabolism. These proteins include the protein translocon protein TIC55, the precursor NADPH:protochlorophyllide oxidoreductase translocon protein PTC52, which operates as protochlorophyllide a-oxygenase, and the lethal leaf spot protein LLS1, which is identical with pheophorbide a oxygenase. The role of these proteins in dark/light regulation and oxidative control by the Trx system is discussed.

SUBMITTER: Bartsch S 

PROVIDER: S-EPMC2290756 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature

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Three thioredoxin targets in the inner envelope membrane of chloroplasts function in protein import and chlorophyll metabolism.

Bartsch Sandra S   Monnet Julie J   Selbach Kristina K   Quigley Françoise F   Gray John J   von Wettstein Diter D   Reinbothe Steffen S   Reinbothe Christiane C  

Proceedings of the National Academy of Sciences of the United States of America 20080318 12

Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge. In their reduced form, they constitute very efficient protein disulfide oxidoreductases. In chloroplasts, two types of Trxs (f and m) coexist and play central roles in the regulation of the Calvin cycle and other processes. Here, we identified a class of Trx targets in the inner plastid envelope membrane of chloroplasts that share a CxxC motif approximately 73 aa from their carboxyl-terminal end. Members of t  ...[more]

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