THE UNCOUPLING PROTEIN FROM BROWN FAT MITOCHONDRIA IS RELATED TO THE MITOCHONDRIAL ADP ATP CARRIER - ANALYSIS OF SEQUENCE HOMOLOGIES AND OF FOLDING OF THE PROTEIN IN THE MEMBRANE
THE UNCOUPLING PROTEIN FROM BROWN FAT MITOCHONDRIA IS RELATED TO THE MITOCHONDRIAL ADP ATP CARRIER - ANALYSIS OF SEQUENCE HOMOLOGIES AND OF FOLDING OF THE PROTEIN IN THE MEMBRANE
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DOI：
10.1002/j.1460-2075.1985.tb03941.x
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发表时间：
1985-01-01
期刊：
影响因子：
11.4
通讯作者：
KLINGENBERG, M
中科院分区：
文献类型：
--
作者：
AQUILA, H;LINK, TA;KLINGENBERG, M
我们在这里报告，第一次，解偶联蛋白的一级结构建立的氨基酸测序。与ADP/ATP载体一样，该蛋白质具有包含三个相似序列的三联结构。每个100个残基。这六个"重复"在可能的结构战略位置上表现出几个残基的惊人保守性，特别是甘氨酸和脯氨酸。虽然这两种蛋白质在氨基酸组成上有很大差异，但它们的序列是远同源的。三个跨膜α-螺旋可以从亲水性图中推导出来。解释两亲性螺旋的修改的图表明5 - 6个这样的α-螺旋。片段此外，两亲性β-可以辨别出跨膜长度链。三分层序结构在亲水性分布上也有明显的反映。基于ADP/ATP载体片段的膜配置，提出了解偶联蛋白多肽链跨膜折叠路径的模型。
We report here, for the first time, the primary structure of uncoupling protein as established by amino acid sequencing. Like the ADP/ATP carrier, this protein has a tripartite structure comprising three similar sequences of .apprx. 100 residues each. These six ''repeats'' exhibit striking conservation of several residues, in particular glycine and proline, at possible structurally strategic positions. Although the two proteins differ strongly in their amino acid composition, their sequences are distantly homologous. Three membrane-spanning .alpha.-helices can be deduced from hydropathy plots. A modified plot accounting for amphiphilic helices indicates 5-6 such .alpha.-segments. In addition an amphiphilic .beta.-strand of membrane-spanning length can be discerned. The tripartite sequence structure is also distinctly reflected in the hydropathy distribution. Based on the membrane disposition of the segments of the ADP/ATP carrier, a model for the transmembrane folding path of the polypeptide chain of the uncoupling protein is proposed.