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Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein
Authors:Zhang Yanfeng  Gao Xiaoli  Michael Garavito R
Affiliation:aCollege of Environmental Science and Engineering, Huazhong University of Science and Technology, Wuhan 430074, PR China;bState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, PR China;cPhotochemistry Laboratory, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, PR China;dHubei Research Institute of Products Quality Supervision and Inspection, Wuhan 430061, PR China
Abstract:In Synechocystis sp. PCC 6803, the loop domain (aa 1–70) of the phycobilisome core-membrane linker, LCM, was found to interact with the glycosyl transferase homolog, Sll1466. Growth of a Sll1466 knock-out mutant was slightly faster in low light, but strongly inhibited in high light; the phenotype is discussed in relation to the regulation of light energy transfer to photosystem II. At the molecular level, the mutant shows the following changes compared to the wild type: (1) a smaller size and higher mobility of phycobilisomes on the thylakoid membrane, and (2) a changed lipid composition of the thylakoid membrane, especially decreased amounts of digalactosyl diacylglycerol. These results indicate a profound regulatory role for Sll1466 in regulating photosynthetic energy transfer.
Keywords:Abbreviations: ApcE, core-membrane linker LCM   DBMIB, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone   DCMU, 3-(3,4-dichlorophenyl)-1,1-dimethylurea   DGDG, digalactosyl diacylglycerol   ET, energy transfer   GT, glycosyl transferase   HL, high light   KPB, potassium phosphate buffer   LL, low light   MGDG, monogalactosyl diacylglycerol   ML, medium light   PAM, pulse amplitude modulated fluorescence   PBS, phycobilisome   PG, phosphatidyl glycerol   PS, photosystem   SQDG, sulfoquinovosyl diacylglycerol   wt, wild type
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