Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural relationship to other mitochondrial transport proteins.
Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural relationship to other mitochondrial transport proteins.
复制标题
牛 2-酮戊二酸/苹果酸载体蛋白的序列：与其他线粒体转运蛋白的结构关系。
作者：
M. Runswick;J. Walker;Fausto Bisaccia;V. Iacobazzi;F. Palmieri
2-酮戊二酸/苹果酸载体蛋白（线粒体内膜的一个组成部分）的氨基酸序列是从重叠的 cDNA 克隆的序列中推导出来的。这些克隆是在聚合酶链式反应中产生的，首先使用寡核苷酸的复杂混合物作为引物和探针，其序列基于纯化蛋白质的溴化氰片段的部分蛋白质序列。载体的蛋白质序列，包括起始子蛋氨酸，长314个氨基酸。成熟蛋白具有修饰的α-氨基，但这种修饰的性质和成熟N端氨基酸的精确位置尚未确定，尽管它必定位于推导的蛋白序列的氨基酸1-4中。将蛋白质序列与其自身以及其他 3 种线粒体载体蛋白（ADP/ATP 转位酶、磷酸盐载体和棕色脂肪解偶联蛋白）的序列进行比较，结果表明，所有 4 种蛋白质均含有长度约为 100 个氨基酸的 3 倍重复序列，并且所有重复都是相互关联的。这表明该蛋白质家族的成员具有相似的结构和机制，并且它们是从共同的起源进化而来的。疏水性氨基酸在氧化戊二酸/苹果酸载体中的分布支持这样的观点，即结构域折叠成相似的结构基序，可能由通过广泛的膜外亲水区域连接的两个跨膜α螺旋组成。还分析了由氧化戊二酸/苹果酸载体基因的较长相关转录本产生的 cDNA 克隆。它们在 3' 非编码区包含 271 个额外的核苷酸。（摘要截断为 250 个字）
The amino acid sequence of the 2-oxoglutarate/malate carrier protein, a component of the inner membranes of mitochondria, has been deduced from the sequences of overlapping cDNA clones. These clones were generated in polymerase chain reactions using, in the first instance, complex mixtures of oligonucleotides as primers and probes, with sequences based upon partial protein sequences of cyanogen bromide fragments of the purified protein. The protein sequence of the carrier, including the initiator methionine, is 314 amino acids long. The mature protein has a modified alpha-amino group, but the nature of this modification and the precise position of the mature N-terminal amino acid have not been ascertained, although it must lie in amino acids 1-4 of the deduced protein sequence. Comparison of the protein sequence with itself and with those of 3 other mitochondrial carrier proteins, ADP/ATP translocase, the phosphate carrier, and the uncoupling protein from brown fat, shows that all 4 proteins contain a 3-fold repeated sequence about 100 amino acids in length, and all the repeats are interrelated. This suggests that the members of this family of proteins have similar structures and mechanisms and that they have evolved from a common origin. The distribution of hydrophobic amino acids in the oxoglutarate/malate carrier supports the view that the domains are folded into similar structural motifs, possibly consisting of two transmembrane alpha-helices joined by an extensive extramembranous hydrophilic region. Clones of cDNA arising from a longer related transcript of the oxoglutarate/malate carrier gene have also been analyzed. They contain 271 additional nucleotides in the 3' noncoding region.(ABSTRACT TRUNCATED AT 250 WORDS)
DOI：
10.1016/s0021-9258(18)61070-1
发表时间：
1987-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
P. Matsudaira
通讯作者：
P. Matsudaira