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Regulation of Chloroplast Membrane Function: Protein Phosphorylation Changes the Spatial Organization of Membrane Components by L A Staehelin; C J Arntzen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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A chlorophyll-protein complex of chloroplast membranes, which simultaneously serves as light-harvesting antenna and membrane adhesion factor, undergoes reversible, lateral diffusion between appressed and nonappressed membrane regions under the control of a protein kinase. The phosphorylation-dependent migration process regulates the amount of light energy that is delivered to the reaction centers of photosystems I and II (PS I and PS II), and thereby regulates their rate of turnover. This regulatory mechanism provides a rationale for the finding that the two photosystems are physically separated in chloroplast membranes (PS II in appressed, grana membranes, and PS I in nonappressed, stroma membranes). The feedback system involves the following steps: a membrane-bound kinase senses the rate of PS II vs. PS I turnover via the oxidation-reduction state of the plastoquinone pool, which shuttles electrons from PS II via cytochrome f to PS I. If activated, the kinase adds negative charge (phosphate) to a grana- localized pigment-protein complex. The change in its surface charge at a site critical for promoting membrane adhesion results in increased electrostatic repulsion between the mem

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Author

L A Staehelin; C J Arntzen

Publisher

Rockefeller University Press.; The Rockefeller University Press; Rockefeller University Press; ScienceOpen (ISSN 0021-9525)

Published

1983

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)