| Literature DB >> 15328351 |
Birgit Klinkert1, Friedrich Ossenbühl, Martha Sikorski, Stefan Berry, Lutz Eichacker, Jörg Nickelsen.
Abstract
The light reactions of oxygenic photosynthesis are mediated by multisubunit pigment-protein complexes situated within the specialized thylakoid membrane system. The biogenesis of these complexes is regulated by transacting factors that affect the expression of the respective subunit genes and/or the assembly of their products. Here we report on the analysis of the PratA gene from the cyanobacterium Synechocystis sp. PCC 6803 that encodes a periplasmic tetratricopeptide repeat protein of formerly unknown function. Targeted inactivation of PratA resulted in drastically reduced photosystem II (PSII) content. Protein pulse labeling experiments of PSII subunits indicated that the C-terminal processing of the precursor of the reaction center protein D1 is compromised in the pratA mutant. Moreover, a direct interaction of PratA and precursor D1 was demonstrated by applying yeast two-hybrid analyses. This suggests that PratA represents a factor facilitating D1 maturation via the endoprotease CtpA. The periplasmic localization of PratA supports a model that predicts the initial steps of PSII biogenesis to occur at the plasma membrane of cyanobacterial cells.Entities:
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Year: 2004 PMID: 15328351 DOI: 10.1074/jbc.M405393200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157