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J. Biol. Chem., Vol. 280, Issue 22, 21667-21672, June 3, 2005
Phycobilisome Linker Proteins Are Phosphorylated in Synechocystis sp. PCC 6803*![]() ![]() ¶
From the
The controversial issue of protein phosphorylation from the photosynthetic apparatus of Synechocystis sp. PCC 6803 has been reinvestigated using new detection tools that include various immunological and in vivo labeling approaches. The set of phosphoproteins detected with these methods includes ferredoxin-NADPH reductase and the linker proteins of the phycobilisome antenna. Using mutants that lack a specific set of linker proteins and are affected in phycobilisome assembly, we show that the phosphoproteins from the phycobilisomes correspond to the membrane, rod, and rod-core linkers. These proteins are in a phosphorylated state within the assembled phycobilisomes. Their dephosphorylation requires partial disassembly of the phycobilisomes and further contributes to their complete disassembly in vitro. In vivo we observed linker dephosphorylation upon long-term exposure to higher light intensities and under nitrogen limitation, two conditions that lead to remodeling and turnover of phycobilisomes. We conclude that this phosphorylation process is instrumental in the regulation of assembly/disassembly of phycobilisomes and should participate in signaling for their proteolytic cleavage and degradation.
Received for publication, November 16, 2004 , and in revised form, February 18, 2005. * This work was supported by Deutsche Forschungsgemeinschaft Grants SFB TR1 and SO 448/2. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. ¶ To whom correspondence should be addressed. Tel.: 49-89-17861242; Fax: 49-891782274; E-mail: Anna.Sokolenko{at}lrz.uni-muenchen.de.
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