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Analysis of chloride-binding domains of the extrinsic 12-kDa protein by proteolysis and directed mutagenesis

机译：通过蛋白水解和定向诱变分析外部12-KDA蛋白的氯化物结合结构域

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Photosynthetic oxygen evolution is catalyzed by the photosystem II (PS II) complex which contains a number of intrinsic membrane-spanning protein components and several extrinsic proteins. The extrinsic proteins are different among cyanobacteria, red algae and higher plants: Higher plant PS II contains the 33-kDa, 23-kDa and 17-kDa proteins, whereas cyanobacterial and red algal PS II contains the 33-kDa, 12-kDa proteins and cytochrome c-550 (cyt c-550) (red algal PS II contains a fourth protein, aunique 20-kDa protein) (Enami et al. 2000). The 12-kDa protein and cyt c-550 in red algal PS II from Cyanidium caldarium play a role in minimizing the chloride and calcium requirement of oxygen-evolving activity, which resembles the function of the 23- and 17-kDa proteins in higher plant PS II (Enami et al. 1998). It was also reported that in Synechocystis PCC 6803, a deletion mutant of the psbU gene encoding the 12-kDa protein grew slower than the wild type under the growth medium lacking Ca~(2+) or Cl~-(Shen et al. 1997). These suggested that the 12-kDa protein of cyanobacterial and red algal PS II functions in minimizing the chloride and calcium requirement for oxygen-evolving activity. The psbU gene coding for the red algal (C. caldarium) 12-kDa protein shows that the mature protein consists of 93 amino acids with a molecular mass of 10,513 Da (Ohta et al. 1999). In order to analyze the functional domains in the 12 kDa protein, we prepared the red algal 12-kDa protein partially lacking its N- and/or C-terminal peptides by limited proteolysis and directed mutagenesis, and examined their binding and reactivating abilities with PS II by means of reconstitution experiments.
机译：光合氧越野被光系统II（PS II）复合物催化，其含有许多内在膜跨越蛋白质组分和几种外在蛋白质。中等蛋白质在蓝藻，红藻类和高等植物中不同：植物PS II含有33-KDA，23-KDA和17-KDA蛋白，而蓝藻和红藻PS II含有33-KDA，12-KDA蛋白和细胞色素C-550（CYT C-550）（红藻PS II含有第四蛋白，Aunique 20-KDA蛋白）（Enami等，2000）。来自Caldarium的红色藻类PS II中的12-KDA蛋白和CYT C-550在最小化氧化活性的氯化物和钙需求中起作用，类似于高等植物中的23和17-KDA蛋白的功能PS II（Enami等人1998）。还报道了，在SyneChocystis PCC 6803中，编码12-KDA蛋白的PSBU基因的缺失突变体比缺乏Ca〜（2+）或Cl〜 - （Shen等人1997的生长培养基下的野生型）。这些表明，蓝藻和红藻PS II的12-KDA蛋白在最小化氯化物和钙需求中的作用，以实现氧化活性。编码用于红色藻类（C.Caldarium）12-KDA蛋白的PSBU基因表明，成熟蛋白质由93个氨基酸组成，其中分子量为10,513 da（Ohta等，1999）。为了分析12kDA蛋白中的功能域，我们制备了通过有限的蛋白水解和定向诱变的缺失其N-和/或C末端肽的红色藻类12-KDA蛋白，并检查了PS的结合和再活化能力二是通过重构实验。

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