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首页> 外文期刊>Biochemistry >Molecular contacts for chlorosome envelope proteins revealed by cross-linking studies with chlorosomes from Chlorobium tepidum
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Molecular contacts for chlorosome envelope proteins revealed by cross-linking studies with chlorosomes from Chlorobium tepidum

机译：氯骨组包蛋白的分子接触通过与氯氯橡胶的氯 - 氯酰胺交联研究显示

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摘要

Chlorosomes are unique light-harvesting antennae found in two phyla of green bacteria: Chlorobi and Chloroflexi. In the green sulfur bacterium Chlorobium tepidum, 10 proteins ( CsmA, CsmB, CsmC, CsmD, CsmE, CsmF, CsmH, CsmI, CsmJ, and CsmX) exist in the chlorosome envelope. Chlorosomes from the wild type and mutants lacking a single chlorosome protein were cross-linked with the zero-length cross-linker 1-ethyl-3-[3-(dimethylamino) propyl] carbodiimide (EDC) and analyzed by gel electrophoresis. Similar cross-linking products were observed when the time and temperature were varied or when EDC was replaced with glutaraldehyde. Specific interactions between chlorosome proteins in cross-linked products were identified by immunoblotting with polyclonal antibodies raised against recombinant chlorosome proteins. We confirmed these interactions by demonstrating that these products were missing in appropriate mutants. Confirming the location of CsmA in the paracrystalline baseplate, cross-linking showed that CsmA forms dimers, trimers, and homomultimers as large as dodecamers and that CsmA directly interacts with the Fenna-Matthews-Olson protein. Cross-linking further suggests that the precursor form of CsmA is inserted near the edges of the baseplate, where CsmA and pre-CsmA interact with CsmB and CsmF. Several chlorosome proteins, including CsmA, CsmC, CsmD, CsmH, CsmI, CsmJ, and CsmX, were shown to exist as homomultimers in the chlorosome envelope. On the basis of the structural information obtained from these cross-linking experiments, a model for the locations and interactions of the proteins of the chlorosome envelope is proposed.
机译：氯代肌是在绿色细菌的两种植物中发现的独特的浅色收获天线：氯吡咯和氯克隆。在氯骨组包络中，在绿色硫磺酸氯橡胶氯橡胶氯橡胶，10个蛋白（CSMA，CSMB，CSMC，CSMD，CSMI，CSMF，CSMX）中存在。来自缺乏单个氯体组蛋白的野生型和突变体的氯体与零长度交联剂1-乙基-3- [3-（二甲基氨基）丙基]碳二亚胺（EDC）交联，并通过凝胶电泳分析。当时间和温度变化或用戊二醛替换EDC时，观察到类似的交联产物。通过免疫印迹与重组氯质蛋白升高的多克隆抗体免疫印迹，鉴定了交联产物中氯体蛋白之间的特异性相互作用。通过证明在适当的突变体中缺少这些产品，我们确认了这些相互作用。确认CSMA在旁丙氨酸底板中的位置，交联表明CSMA形成二聚体，三聚体和同源体，与DoDecamer一样大，并且CSMA直接与Fenna-Matthews-Olson蛋白相互作用。交联进一步表明CSMA的前体形式插入底板的边缘附近，其中CSMA和Pre-CSMA与CSMB和CSMF相互作用。几种氯体组蛋白，包括CSMA，CSMC，CSMSMD，CSMH，CSMI，CSMJ和CSMX，作为氯运动组包络中的同源体存在。基于从这些交联实验获得的结构信息，提出了一种用于氯运动组封套蛋白的位置和相互作用的模型。

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