Mitochondrial metabolite transporters

Mitochondrial metabolite transporters
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DOI:
10.1016/0005-2728(96)00062-x
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发表时间:
1996-07-18
影响因子:
4.3
通讯作者:
Palmieri, L
Palmieri, L
中科院分区:
生物学2区
文献类型:
--
作者:
Palmieri, F;Bisaccia, F;Palmieri, L

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线粒体载体是线粒体内膜的固有蛋白,其催化代谢物跨膜运输,并且不仅对于氧化磷酸化而且对于所有代谢途径都是必需的,其酶在线粒体内和线粒体外空间之间分配。到目前为止,已经纯化了10种线粒体载体(其中7种在我们的实验室中),并将其功能性重组为脂质体(综述见[1,2])。这些转运蛋白是来自棕色脂肪的解偶联蛋白和ADP/ATP、磷酸盐、酮戊二酸盐、柠檬酸盐、二羧酸盐、丙酮酸盐、肉毒碱、天冬氨酸盐/谷氨酸盐和鸟氨酸载体。这些生化表征的转运蛋白中的前五种的一级结构已通过氨基酸分析或DNA测序确定(综述见[1])。这些蛋白质由三个相关的序列组成,长度约为100个氨基酸。每个重复元件包含两个由广泛的亲水区域分隔的疏水段。此外,每种蛋白质的重复序列与其他蛋白质中存在的重复序列相关。三重结构、每个结构域中两个疏水区的存在以及特定序列基序的三倍重复表明,这五种线粒体载体属于一个单一的载体蛋白家族,由一个共同的祖先通过双串联基因复制进化而来。上述线粒体载体的特征性序列特征也已在许多已知序列但功能未知的其他蛋白质中发现,因此这些蛋白质被包括在同一蛋白质家族中(综述参见[1])。通过考试-
The mitochondrial carriers are intrinsic proteins of the inner membranes of mitochondria that catalyze the transport of metabolites across the membrane and are necessary not only for oxidative phosphorylation but also for all the metabolic pathways, whose enzymes are partitioned between the intra-and the extramitochondrial space. So far, ten mitochondrial carriers (seven of which in our laboratory) have been purified and functionally reconstituted into liposomes (for reviews see [1, 2]). These transporters are the uncoupling protein from brown fat and the ADP/ATP, phosphate, oxoglutarate, citrate, dicarboxylate, pyruvate, carnitine, aspartate/glutamate and ornithine carriers. The primary structure of the first five of these biochemically characterized transporters has been determined by amino acid analysis or DNA sequencing (for a review see [1]). These proteins are made up of three related sequences about 100 amino acids in length. Each repetitive element contains two hydrophobic stretches separated by an extensive hydrophilic region. Furthermore, the repeats of each protein are related to those present in the others. The tripartite structure, the presence of the two hydrophobic regions in each domain and the three-fold repetition of a particular sequence motif show that these five mitochondrial carriers belong to a single carrier protein family, evolved from a common ancestor by two-tandem gene duplication. The characteristic sequence features of the above-mentioned mitochondrial carriers have also been found in a number of other proteins of known sequence but of unknown function, which are therefore included in the same protein family (for a review see [1]). By examina-