首页> 外文期刊>Biochimica et biophysica acta. Bioenergetics >Salt shock-inducible Photosystem I cycle electron transfer in Synechocystis PCC6803 relies on binding of ferredoxin: NADP~+ reductase to the thylakoid membranes via its CpcD phycobilisome-linker homologous N-terminal domain
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Salt shock-inducible Photosystem I cycle electron transfer in Synechocystis PCC6803 relies on binding of ferredoxin: NADP~+ reductase to the thylakoid membranes via its CpcD phycobilisome-linker homologous N-terminal domain

机译:盐胁迫诱导的光系统I周期集胞藻PCC6803中的电子转移依赖于铁氧还蛋白:NADP〜+还原酶通过其CpcD藻胆体-接头同源N端结构域与类囊体膜结合。

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摘要

Relative to ferredoxin: NADP~+ reductase (FNR) from chloroplasts, the comparable enzyme in cyanobacteria contains an additional 9 kDa domain at its amino-terminus. The domain is homologous to the phycocyanin associated linker polypeptide CpcD of the light harvesting phycobilisome antennae. The phenotypic consequences of the genetic removal of this domain from the petH gene, which encodes FNR, have been studied in Synechocystic PCC 6803. The in frame deletion of 75 residues at the amino-terminus, rendered chloroplast length FNR enzyme with normal functionality in linear photosynthetic electron transfer. Salt shock correlated with increased abundance of petH mRNA in the wild-type and mutant alike. The truncation stopped salt stress-inducible increase of Photosystem I-dependent cyclic electron flow. Both photoacoustic determination of the storage of energy from Photosystem I specific far-red light, and the re-reduction kinetics of P700~+, suggest lack of function of the truncated FNR in the plastoquinone-cytochrome b_6f complex reductase step of the PS I-dependent cyclic electron transfer chain. Independent gold-immunodecoration studies and analysis of FNR distribution through activity staining after native polyacrylamide gelelectrophoresis showed that association of FNR with the thylakoid membranes of Synechocystis PCC 6803 requires the presence of the extended amino-terminal domain of the enzyme. The truncated ΔpetH gene was also transformed into a NAD(P)H dehydrogenase (NDH1) deficient mutant of Synechocystis PCC 6803 (strain M55) (T. Ogawa, Proc. Natl. Acad. Sci. USA 88 (1991) 4275 - 4279). Phenotypic characterisation of the double mutant supported our conclusion that both the NAD(P)H dehydrogenase complex and FNR contribute independently to the quinone cytochrome b_6f reductase step in PS I-dependent cyclic electron transfer. The distribution, binding properties and function of FNR in the model cyanobacterium Synechocystic PCC 6803 will be discussed.
机译:相对于来自叶绿体的铁氧还蛋白:NADP〜+还原酶(FNR),蓝细菌中的可比酶在其氨基末端还包含一个额外的9 kDa结构域。该结构域与光收集藻胆体触角的藻蓝蛋白相关的接头多肽CpcD同源。已在Synechocystic PCC 6803中研究了从编码FNR的petH基因中遗传去除该结构域的表型后果。在氨基末端框内缺失75个残基,使叶绿体长度FNR酶具有线性的正常功能光合电子转移。盐冲击与野生型和突变型中petH mRNA丰度的增加有关。截断停止了盐胁迫诱导的光系统I依赖性循环电子流的增加。光声法测定光系统I特定远红外光的能量存储,以及P700〜+的还原动力学都表明PS I-的质体醌-细胞色素b_6f复合还原酶步骤中截短的FNR功能不足。依赖性环状电子转移链。独立的金免疫装饰研究和天然聚丙烯酰胺凝胶电泳后通过活性染色对FNR分布的分析表明,FNR与突囊藻PCC 6803的类囊体膜缔合需要存在该酶的扩展氨基末端结构域。截短的ΔpetH基因也被转化为集胞藻PCC 6803(菌株M55)的NAD(P)H脱氢酶(NDH1)缺陷型突变体(T. Ogawa,Proc.Natl.Acad.Sci.USA 88(1991)4275-4279) 。双突变体的表型表征支持我们的结论,即NAD(P)H脱氢酶复合物和FNR都独立地参与了PS I依赖的循环电子转移中的醌细胞色素b_6f还原酶步骤。将讨论模型蓝藻蓝藻PCC 6803中FNR的分布,结合特性和功能。

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