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首页> 外文期刊>Scientific reports. >Lumenal exposed regions of the D1 protein of PSII are long enough to be degraded by the chloroplast Deg1 protease
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Lumenal exposed regions of the D1 protein of PSII are long enough to be degraded by the chloroplast Deg1 protease

机译：PSII的D1蛋白的腔外暴露区域足够长，可以通过叶绿体DEG1蛋白酶降解

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摘要

Degradation of the D1 protein of photosystem II (PSII) reaction center is a pre-requisite for the repair cycle from photoinhibition. Two types of thylakoid proteases, FtsH and Deg, have been demonstrated to participate in this process. However, the location of the proteolytic sites of the lumenal Deg1 protease within its internal sphere raised the question whether the lumenal-exposed regions of D1 are indeed long enough to reach these sites. Implanting these regions into the stable GFP rendered it sensitive to the presence of Deg1 in vitro, demonstrating that the flexible regions of D1 that protrude into the lumen can penetrate through the three side-openings of Deg1 and reach its internal proteolytic sites. This mode of action, facilitating cooperation between proteases on both sides of the thylakoid membranes, should be applicable to the degradation of other integral thylakoid membrane proteins as well.
机译：照相系统II（PSII）反应中心的D1蛋白的降解是从光抑制的修复周期的预先确定。已经证明了两种类型的类蛋白蛋白酶，FTSH和DEG参与了该过程。然而，在其内部球体内的腔Deg1蛋白酶的蛋白水解位点的位置提出了D1的腔暴露区域是否确实足够长以达到这些位点。将这些区域植入稳定的GFP使其对体外DEG1的存在敏感，表明突出到腔中的D1的柔性区域可以穿透DEG1的三个侧开口并达到其内部蛋白水解位点。这种作用模式，促进蛋白酶在紫花状膜两侧之间的合作，也应适用于其他整体的囊体膜蛋白的降解。

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