Environmentally modulated phosphorylation and dynamics of proteins in photosynthetic membranes
2007 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, Vol. 1767, no 6, 449-457 p.Article in journal (Refereed) Published
Recent advances in vectorial proteomics of protein domains exposed to the surface of photosynthetic thylakoid membranes of plants and the green alga Chlamydomonas reinhardtii allowed mapping of in vivo phosphorylation sites in integral and peripheral membrane proteins. In plants, significant changes of thylakoid protein phosphorylation are observed in response to stress, particularly in photosystem II under high light or high temperature stress. Thylakoid protein phosphorylation in the algae is much more responsive to the ambient redox and light conditions, as well as to CO2 availability. The light-dependent multiple and differential phosphorylation of CP29 linker protein in the green algae is suggested to control photosynthetic state transitions and uncoupling of light harvesting proteins from photosystem II under high light. The similar role for regulation of the dynamic distribution of light harvesting proteins in plants is proposed for the TSP9 protein, which together with other recently discovered peripheral proteins undergoes specific environment- and redox-dependent phosphorylation at the thylakoid surface. This review focuses on the environmentally modulated reversible phosphorylation of thylakoid proteins related to their membrane dynamics and affinity towards particular photosynthetic protein complexes. © 2006 Elsevier B.V. All rights reserved.
Place, publisher, year, edition, pages
2007. Vol. 1767, no 6, 449-457 p.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-39483DOI: 10.1016/j.bbabio.2006.11.007Local ID: 48928OAI: oai:DiVA.org:liu-39483DiVA: diva2:260332