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首页> 外文期刊>Molecular and Cellular Biology >A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase complexed with chlorophyllide.
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A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase complexed with chlorophyllide.

机译：大麦质体的光诱导蛋白酶降解与叶绿素复合的NADPH：原叶绿素氧化还原酶。

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摘要

The NADPH:protochlorophyllide oxidoreductase precursor protein (pPorA) of barley (Hordeum vulgare L. cv. Carina), synthesized from a full-length cDNA clone by coupling in vitro transcription and translation, is a catalytically active protein. It converts protochlorophyllide to chlorophyllide in a light- and NADPH-dependent manner. At least the pigment product of catalysis remains tightly bound to the precursor protein. The chlorophyllide-pPorA complex differs markedly from the protochlorophyllide-pPorA complex with respect to sensitivity to attack by a light-induced, nucleus-encoded, and energy-dependent protease activity of barley plastids. The pPorA-chlorophyllide complex is rapidly degraded, in contrast to pPorA-protochlorophyllide complexes containing or lacking NADPH, which are both resistant to protease treatment. Unexpectedly, pPorA devoid of its substrates or products was less sensitive to proteolysis than the pPorA-chlorophyllide complex, suggesting that both substrate binding and product formation during catalysis had caused differential changes in protein conformation.
机译：大麦（Hordeum vulgare L. cv。Carina）的NADPH：原叶绿素内酯氧化还原酶前体蛋白（pPorA）是由全长cDNA克隆通过体外转录和翻译偶联合成的，是一种催化活性蛋白。它以光和NADPH依赖性方式将原叶绿素内酯转化为叶绿素内酯。至少催化的色素产物保持与前体蛋白紧密结合。叶绿素-pPorA复合物与原叶绿素-pPorA复合物在对大麦质体的光诱导，核编码和能量依赖的蛋白酶活性的攻击敏感性方面有显着差异。与包含或缺乏NADPH的pPorA-叶绿素前体复合物相比，pPorA-叶绿素前体复合物均被快速降解，两者均对蛋白酶处理具有抗性。出乎意料的是，没有其底物或产物的pPorA对蛋白水解的敏感性不如pPorA-叶绿素复合物，这表明底物结合和催化过程中产物的形成均引起蛋白质构象的差异性变化。

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