首页> 美国卫生研究院文献>Scientific Reports >Lumenal exposed regions of the D1 protein of PSII are long enough to be degraded by the chloroplast Deg1 protease
【2h】

Lumenal exposed regions of the D1 protein of PSII are long enough to be degraded by the chloroplast Deg1 protease

机译:PSII D1蛋白的腔暴露区域足够长足以被叶绿体Deg1蛋白酶降解

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

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:光系统II(PSII)反应中心的D1蛋白的降解是光抑制修复周期的先决条件。已证明两种类囊体蛋白酶FtsH和Deg参与该过程。然而,管腔Deg1蛋白酶的蛋白水解位点在其内部球体内的位置提出了一个问题,即D1的管腔暴露区域是否确实足够长以到达这些位点。将这些区域植入稳定的GFP使其在体外对Deg1的存在敏感,表明突出到管腔中的D1柔性区域可以穿透Deg1的三个侧面开口并到达其内部蛋白水解位点。这种作用方式,促进类囊体膜两侧的蛋白酶之间的协同作用,也应适用于其他整体类囊体膜蛋白的降解。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号