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首页> 外文期刊>Biochemistry >Degradation of Antenna Ghlorophyll-Binding Protein CP43 during Photoinhibition of Photosystem II
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Degradation of Antenna Ghlorophyll-Binding Protein CP43 during Photoinhibition of Photosystem II

机译：光系统II的光抑制过程中天线Ghlorophyll结合蛋白CP43的降解。

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When photosystem II (PS II) membranes from spinach were treated with Tris (0.8 M, pH 9 0) and illuminated with white light (5000 μE m~(-2) s~(-1)) under aerobic conditions at 25 °C, not only were the reaction centei-forming Dl and D2 proteins degraded but the antenna chlorophyll-binding protein CP43 was also degraded. Three products of the degradation of CP43, with molecular masses of 17 0, 15 5, and 14 kDa, respectively, were identified by sodium dodecyl sulfate/urea polyacrylamide gel electrophoresis and Western blotting with a specific antibody. Degradation products of another antenna chlorophyll-binding protein of PS II, CP47, were not detected under the same conditions Concomitant with the damage to the Dl and D2 proteins and CP43, cross-linked products of the DTprotein, CP43, and CP47 were formed. These products were identified as slow-moving smeared bands in the higher molecular weight range of the gel during electrophoresis. Both the degradation and the cross-linking of these proteins were prevented by the addition of electron donors to PS II, a result that suggests that these processes were caused 'by the donor-side mechanism of photoinhibition. The photoinduced degradation of CP43 and the cross-linking among the Dl protein, CP43, and CP47 were less obvious in the PS II membranes that had been treated with hydroxylamine rather fhan Tris and in the membranes that had been treated with Tris and reconstituted by addition of an extrinsic 33-kDa protein (OEC33) These results indicate that removal of OEC33, which is closely associated with CP43, from the PS II complex accelerates the degradation and cross-linking of CP43 during photoinhibition. It is suggested that OEC33 is involved in the stabilization of the antenna chlorophyll-binding proteins in PS II during photoinhibition.
机译：当菠菜的光系统II（PS II）膜用Tris（0.8 M，pH 9 0）处理并在25°C有氧条件下用白光（5000μEm〜（-2）s〜（-1））照射时。不仅形成反应的半抗原的D1和D2蛋白被降解，触角叶绿素结合蛋白CP43也被降解。通过十二烷基硫酸钠/尿素聚丙烯酰胺凝胶电泳和特异抗体的Western印迹鉴定了三种降解CP43的产物，其分子量分别为17 0、15 5和14 kDa。在相同条件下未检测到PS II的另一种天线叶绿素结合蛋白CP47的降解产物，伴随D1和D2蛋白和CP43的破坏，形成了DTprotein，CP43和CP47的交联产物。在电泳过程中，这些产物在凝胶的较高分子量范围内被识别为缓慢移动的条带。这些蛋白质的降解和交联都可以通过在PS II中添加电子供体来防止，结果表明这些过程是“由光抑制的供体侧机制引起的”。 CP43的光诱导降解以及Dl蛋白，CP43和CP47之间的交联在用羟胺而不是Tris处理的PS II膜中以及在用Tris处理并通过加成还原的膜中不太明显。外源性33-kDa蛋白（OEC33）的合成这些结果表明，从PS II复合物中除去与CP43密切相关的OEC33会加速光抑制过程中CP43的降解和交联。建议OEC33在光抑制过程中参与PS II中叶绿素结合蛋白的稳定化。

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