外质体包膜蛋白Oep16：作为原叶绿素酸酯氧化还原酶A导入过程中的前体转位酶的作用。
The outer plastid envelope protein Oep16: role as precursor translocase in import of protochlorophyllide oxidoreductase A.
作者信息
Reinbothe Steffen, Quigley Françoise, Springer Armin, Schemenewitz Andreas, Reinbothe Christiane
机构信息
Université Joseph Fourier et Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5575, BP53, F-38041 Grenoble Cedex 9, France.
出版信息
Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):2203-8. doi: 10.1073/pnas.0301962101. Epub 2004 Feb 9.
Abstract
A 16-kDa plastid envelope protein was identified by chemical crosslinking that interacts with the precursor of NADPH:protochlorophyllide oxdidoreductase A (pPORA) during its posttranslational import into isolated barley chloroplasts. Protein purification and subsequent protein sequencing showed that the 16-kDa protein is an ortholog of a previously identified outer plastid envelope protein, Oep16. A protein of identical size was present in barley etioplasts and interacted with pPORA. Similar 16-kDa protein-dependent crosslink products of pPORA were detected in wheat, pea, and Arabidopsis chloroplasts. Database analyses revealed that the 16-kDa protein belongs to a family of preprotein and amino acid transporters found in free-living bacteria and endosymbiotic mitochondria and chloroplasts. Antibodies raised against the 16-kDa protein inhibited import of pPORA, highlighting its role in protein import.
摘要
通过化学交联鉴定出一种16 kDa的质体包膜蛋白，在NADPH：原叶绿素酸氧化还原酶A（pPORA）翻译后导入分离的大麦叶绿体的过程中，该蛋白与pPORA的前体相互作用。蛋白质纯化及后续的蛋白质测序表明，16 kDa的蛋白是先前鉴定出的外质体包膜蛋白Oep16的直系同源物。大麦黄化质体中存在大小相同的蛋白，且该蛋白与pPORA相互作用。在小麦、豌豆和拟南芥叶绿体中检测到了类似的依赖16 kDa蛋白的pPORA交联产物。数据库分析表明，16 kDa的蛋白属于在自由生活细菌以及内共生线粒体和叶绿体中发现的前体蛋白和氨基酸转运蛋白家族。针对16 kDa蛋白产生的抗体抑制了pPORA的导入，突出了其在蛋白质导入中的作用。
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