4.6 Article

V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus -: Subunit structure and operon

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JOURNAL OF BIOLOGICAL CHEMISTRY
卷 275, 期 18, 页码 13955-13961

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AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.275.18.13955

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V-type ATPase (VoV1) capable of ATP-driven H+ pumping and of H+ gradient driven ATP synthesis was isolated from a thermophilic eubacterium, Thermus thermophilus. When the enzyme was analyzed by gel electrophoresis in the presence of sodium dodecyl sulfate, it showed eight polypeptide bands of which four were subunits of V-1. We also isolated the VoV1 operon, containing nine genes in the order of atpG-I-L-E-X-F-A-B-D), which encoded proteins with molecular sizes of 13, 43, 10, 20, 35, 11, 64, 53, and 25 kDa, respectively. The last four genes were identified as those for V-1 subunits; atpA, B, D, and F encoded the A, B, gamma, and delta subunits, respectively. The first five genes, atpG-atpX, were identified as genes for the V-o subunits. The product of atpL, the proteolipid subunit, lacked a 19-amino acid presequence and, unlike V-type ATPases, contained two membrane-spanning domains rather than four. The hydrophobic 43-kDa product of atpI is the smallest member so far found of the eukaryotic 100-kDa subunit family. Its electrophoretic band overlapped with the band of the A subunit. Therefore, all the gene products were found in our purified VoV1. We isolated the A(3)B(3) subcomplex reconstituted from the isolated subunits and the A(3)B(3)gamma subcomplex from subunit-expressing Escherichia coli. Electron microscopic observation of these subcomplexes revealed that the gamma subunit of V-1 filled the central cavity of A,B, and might be central subunit, similar to the gamma subunit of F-1-ATPase.

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