کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298904 | 1537049 | 2010 | 15 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mitochondrial carriers function as monomers
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کلمات کلیدی
AFMBN-PAGEBKACATRC12E8CarboxyatractylosideBongkrekic acid - اسید بونکروکیکSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدProtein–protein interaction - تعامل پروتئین-پروتئینOligomeric state - حالت OligomericLipid - لیپیدDetergent - مواد شویندهTransport mechanism - مکانیزم حمل و نقلatomic force microscopy - میکروسکوپ نیروی اتمیMembrane protein - پروتئین غشائی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
Mitochondrial carriers link biochemical pathways in the mitochondrial 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 35Â 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 817-831
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 817-831
نویسندگان
Edmund R.S. Kunji, Paul G. Crichton,