Escherichia coli H+-ATPase: Role of the δ subunit in binding F1 to the F0 sector

Escherichia coli H+-ATPase: Role of the δ subunit in binding F1 to the F0 sector
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大肠杆菌 H+-ATP 酶:δ 亚基在 F1 与 F0 区域结合中的作用

DOI:
10.1016/0003-9861(92)90005-h
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发表时间:
1992
影响因子:
3.9
通讯作者:
M. Futai
M. Futai
中科院分区:
生物学3区
文献类型:
--
作者:
M. Jounouchi;M. Takeyama;P. Chaiprasert;T. Noumi;Y. Moriyama;M. Maeda;M. Futai

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通过突变体分析,研究了大肠杆菌H ~+-ATP酶(F0 F1)δ亚基(177个氨基酸残基)的功能。无义突变体(Gln-23 → end,Gln-29 → end,Gln-74 → end)和错义突变体(Gly-150 → Asp)的膜ATP酶活性很低,表明δ亚基是F1部分与F0结合所必需的。Gln-176 → end突变体的膜结合活性与野生型基本相同,而在瓦尔-174 → end突变体中,大部分ATP酶活性位于细胞质中。因此,瓦尔-174(也可能是Leu-175)对于维持亚基的结构是必需的,而两个羧基末端残基Gln-176和Ser-177是不稳定的。在各种残基(Thr-11、Glu-26、Asp-30、Glu-42、Glu-82、Arg-85、Asp-144、Arg-154、Asp-161、Ser-163)处引入取代,包括明显保守的亲水性残基。所得突变体具有与野生型基本上相同的表型,表明这些残基不具有任何显著的功能作用。突变分析(Gly-150 → Asp、Pro或Ala)表明Gly-150本身不是必需的,但突变可能影响亚基的结构。这些结果表明,δ亚基的整体结构是必要的,但个别残基可能没有严格的功能作用。
The roles of theEscherichia coliH+-ATPase (F0F1) δ subunit (177 amino acid residues) was studied by analyzing mutants. The membranes of nonsense (Gln-23 → end, Gln-29 → end, Gln-74 → end) and missense (Gly-150 → Asp) mutants had very low ATPase activities, indicating that the δ subunit is essential for the binding of the F1portion to F0. The Gln-176 → end mutant had essentially the same membrane-bound activity as the wild type, whereas in the Val-174 → end mutant most of the ATPase activity was in the cytoplasm. Thus Val-174 (and possibly Leu-175 also) was essential for maintaining the structure of the subunit, whereas the two carboxyl terminal residues Gln-176 and Ser-177 were dispensable. Substitutions were introduced at various residues (Thr-11, Glu-26, Asp-30, Glu-42, Glu-82, Arg-85, Asp-144, Arg-154, Asp-161, Ser-163), including apparently conserved hydrophilic ones. The resulting mutants had essentially the same phenotypes as the wild type, indicating that these residues do not have any significant functional role(s). Analysis of mutations (Gly-150 → Asp, Pro, or Ala) indicated that Gly-150 itself was not essential, but that the mutations might affect the structure of the subunit. These results suggest that the overall structure of the δ subunit is necessary, but that individual residues may not have strict functional roles.
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DOI: --
发表时间: 1989
期刊: The Journal of biological chemistry
影响因子: --
作者:
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大肠杆菌 F1F0-ATP 合酶的交联和标​​记揭示了 F0 靠近 F1 催化亚基的紧凑亲水部分。
DOI: --
发表时间: 1983
期刊: The Journal of biological chemistry
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通讯作者: Simoni,RD
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DOI: --
发表时间: 1990
期刊: The Journal of biological chemistry
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作者:
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通讯作者: Mueller,DM