期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1797, 期 6-7, 页码 817-831出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2010.03.023
关键词
Membrane protein; Oligomeric state; Transport mechanism; Detergent; Lipid; Protein-protein interaction
资金
- Medical Research Council [MC_U105663139] Funding Source: Medline
- MRC [MC_U105663139] Funding Source: UKRI
- Medical Research Council [MC_U105663139] Funding Source: researchfish
Mitochondrial carriers link biochemical pathways in the mitochondria( matrix and cytosol by transporting metabolites, inorganic ions, nucleotides and cofactors across the mitochondrial inner membrane. Uncoupling proteins that dissipate the proton electrochemical gradient also belong to this protein family. For almost 35 years the general consensus has been that mitochondrial carriers are dimeric in structure and function. This view was based on data from inhibitor binding studies, small-angle neutron scattering, electron microscopy, differential tagging/affinity chromatography, size-exclusion chromatography, analytical ultracentrifugation, native gel electrophoresis, cross-linking experiments, tandem-fusions, negative dominance studies and mutagenesis. However, the structural folds of the ADP/ATP carriers were found to be monomeric, lacking obvious dimerisation interfaces. Subsequently, the yeast ADP/ATP carrier was demonstrated to function as a monomer. Here, we revisit the data that have been published in support of a dimeric state of mitochondrial carriers. Our analysis shows that when critical factors are taken into account, the monomer is the only plausible functional form of mitochondrial carriers. We propose a transport model based on the monomer, in which access to a single substrate binding site is controlled by two flanking salt bridge networks, explaining uniport and strict exchange of substrates. (C) 2010 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据