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Regulation of Synthesis of PSI in the Cyanophytes Synechocystis PCC6714 and Plectonema boryanum during the Acclimation of the Photosystem Stoichiometry to the Light Quality
Authors:Aizawa, Katsunori   Fujita, Yoshihiko
Affiliation:Department of Cell Biology, National Institute for Basic Biology Okazaki, Aichi, 444 Japan
Abstract:The effects of light quality on the formation of the PSI complexwere examined in Synechocystis PCC6714 and in Plectonema boryanum.The rate of increase in levels of core polypeptides of PSI,PsaA/B, doubled upon shift from Chl a-absorbed light (PSI light)to phycobilisome-ab-sorbed light (PSII light). The elevatedrate was decreased upon the reverse shift. Half time of theacceleration was approximately 10 min, and that of the decreasewas approximately 4 min. The rate of degradation of the polypeptideswas far lower than the rate of the increase under either lightregime. Neither synthesis nor degradation of the PsbA and PsbCpolypeptides of PSII was significantly altered by the lightquality. We conclude that synthesis of the PSI complex is chromaticallyregulated to allow adjustments in photosystem stoichiometry.The level of mRNA for PsaA/B was not altered by the light regime.Anomalous inhibition by chloramphenicol suggested that the regulationoccurs at a step(s) other than the peptide elongation step,perhaps at the initiation of the ribosome cycle or at the insertionof Chl a for the stabilization of the polypeptides. The pho-toreductionof protochlorophyllide (Pchlide) was compared with the synthesisof the polypeptides in a mutant of Plectonema boryanum thatlacked Pchlide dark reductase (YFC1004). The results indicatedthat the synthesis of stable PsaA/B polypeptides was not limitedby the reduction of Pchlide, although the synthesis did dependon a supply of Chl a. 1Present address: Department of Plant Biology, University ofMaryland at College Park, MD 20742, U.S.A.2Present address: Department of Marine Bioscience, Fukui Pre-fecturalUniversity, Obama, Fukui, 917 Japan
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