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Plant Physiology Preview Published on June 23, 2006; 10.1104/pp.106.082339
Received April 18, 2006 Iron Deficiency in Cyanobacteria Causes Monomerization of PSI Trimers and Reduces the Capacity for State Transitions and the Effective Absorption Cross Section of PSI In Vivo
Department of Biology and The Biotron, University of Western Ontario, 1151 Richmond Street N., London, Ontario, Canada N6A 5B7; Department of Plant Physiology, University of Umeå, Umeå S-901 87, Sweden * Corresponding author; email: nhuner{at}uwo.ca.
The induction of the isiA (CP43') protein in iron-stressed cyanobacteria is accompanied by the formation of a ring of 18 CP43' proteins around the PSI trimer and is thought to increase the absorption cross section of PSI within the CP43'-PSI supercomplex. In contrast to these in vitro studies, our in vivo measurements failed to demonstrate any increase of the PSI absorption cross section in two strains (Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803) of iron-stressed cells. We report that Fe-stressed cells exhibited a reduced capacity for state transitions and limited dark reduction of the plastoquinone (PQ) pool, which accounts for the increase in PSII-related 685 nm Chl fluorescence under Fe-deficiency. This was accompanied by lower abundance of the NADP-dehydrogenase complex (Ndh-H) and the PSI associated polypeptide PsaL, as well as a reduced amount of phosphatidylglycerol (PG). Non-denaturating PAGE separation of the Chl-protein complexes indicated that the monomeric form of PSI is favoured over the trimeric form of PSI under Fe-stress. Thus, we demonstrate that the induction of CP43' does not increase the PSI functional absorption cross section of whole cells in vivo, but rather, induces monomerization of PSI trimers and reduces the capacity for state transitions. We discuss the role of CP43' as an effective energy quencher to photoprotect PSII and PSI under unfavorable environmental conditions in cyanobacteria in vivo.
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