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Published on March 2, 2007; 10.1104/pp.107.096396

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Received January 23, 2007
Accepted February 22, 2007

REP27, a Tetratricopeptide Repeat Nuclear-encoded and Chloroplast-localized Protein Functions in the D1/32 kD Reaction Center Protein Turnover and PSII Repair from Photodamage

Sungsoon Park , Phichaya Khamai , Jose Gines Garcia-Cerdan , and Anastasios Melis *

Department of Plant and Microbial Biology, University of California, Berkeley, CA, 94720-3102, USA

* Corresponding author; email: melis{at}nature.berkeley.edu.

The goal of this research is elucidation of the molecular mechanism for the unique photosystem-II (PSII) damage and repair cycle in chloroplasts. A frequently occurring irreversible photo-oxidative damage inhibits the PSII charge separation reaction and stops photosynthesis. The chloroplast PSII repair process rectifies this adverse effect by selectively removing and replacing the photo-inactivated D1/32 kD reaction center protein (the chloroplast-encoded psbA gene product) from the massive (>1,000 kD) H2O-oxidizing and O2-evolving PSII holocomplex. DNA insertional mutagenesis in the model organism Chlamydomonas reinhardtii was applied for the isolation and characterization of rep27, a repair-aberrant mutant. Gene cloning and biochemical analyses in this mutant resulted in the identification of REP27, a nuclear gene encoding a putative chloroplast-targeted protein, which is specifically required for the completion of the D1 turnover process, but is not essential for the de novo biogenesis and assembly of the PSII holocomplex in this model green alga. The REP27 protein contains two highly conserved tetratricopeptide repeats, postulated to facilitate the psbA mRNA co-translational insertion of the nascent D1 protein in the existing PSII core template. Elucidation of the PSII repair mechanism may reveal the occurrence of hitherto unknown regulatory and catalytic reactions for the selective in situ replacement of specific proteins from within multi-protein complexes.






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