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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
Institution: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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