Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II.

Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II.
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CP43无光系统II的亚基组成,Synechocystis sp。 PCC 6803:对光系统II的组装和修复的影响。

DOI:
10.1098/rstb.2012.0066
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发表时间:
2012-12-19
期刊:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
影响因子:
--
通讯作者:
Nixon PJ
Nixon PJ
中科院分区:
其他
文献类型:
--
作者:
Boehm M;Yu J;Reisinger V;Beckova M;Eichacker LA;Schlodder E;Komenda J;Nixon PJ

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光系统II(PSII)突变体是有用的实验工具,以捕获潜在的中间体参与组装的放氧PSII复合物。在这里,我们专注于RC 47组装复合物的亚基组合物,积累在一个psbC无效突变的蓝藻集胞藻属PCC 6803不能使CP 43 apopeptide。通过使用天然凝胶电泳,我们表明RC 47是异质性的,主要是作为220 kDa的单体发现的。RC 47复合物与小Cab样蛋白(ScpC和/或ScpD)以及Psb 28及其同源物Psb 28 -2共纯化。分离的His-标记的RC 47的分析表明,存在的D1,D2,CP 47 apopolypeptide,加上9的13个低分子量(LMM)亚基中发现的PSII全酶,包括PsbL,PsbM和PsbT,这是在两个单体之间的界面上的二聚体全酶。未检测到位于全酶中CP 43附近的LMM亚基(PsbK、PsbZ、Psb 30和PsbJ)。分离的RC 47-His复合物的光化学活性,包括P680+的还原速率,与缺少Mn 4CaO 5簇的PSII复合物的光化学活性相似。我们的研究结果的组装和修复PSII在体内的影响进行了讨论。
Photosystem II (PSII) mutants are useful experimental tools to trap potential intermediates involved in the assembly of the oxygen-evolving PSII complex. Here, we focus on the subunit composition of the RC47 assembly complex that accumulates in a psbC null mutant of the cyanobacterium Synechocystis sp. PCC 6803 unable to make the CP43 apopolypeptide. By using native gel electrophoresis, we showed that RC47 is heterogeneous and mainly found as a monomer of 220 kDa. RC47 complexes co-purify with small Cab-like proteins (ScpC and/or ScpD) and with Psb28 and its homologue Psb28-2. Analysis of isolated His-tagged RC47 indicated the presence of D1, D2, the CP47 apopolypeptide, plus nine of the 13 low-molecular-mass (LMM) subunits found in the PSII holoenzyme, including PsbL, PsbM and PsbT, which lie at the interface between the two momomers in the dimeric holoenzyme. Not detected were the LMM subunits (PsbK, PsbZ, Psb30 and PsbJ) located in the vicinity of CP43 in the holoenzyme. The photochemical activity of isolated RC47-His complexes, including the rate of reduction of P680+, was similar to that of PSII complexes lacking the Mn4CaO5 cluster. The implications of our results for the assembly and repair of PSII in vivo are discussed.
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