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
中科院分区:
文献类型:
--
作者:
Palmieri, F;Bisaccia, F;Palmieri, L
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-