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
复制标题
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
复制
发表时间:
1992
影响因子:
3.9
通讯作者:
M. Futai
中科院分区:
文献类型:
--
作者:
M. Jounouchi;M. Takeyama;P. Chaiprasert;T. Noumi;Y. Moriyama;M. Maeda;M. Futai
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.
DOI:
--
发表时间:
1989
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Brusilow,WS;Scarpetta,MA;Hawthorne,CA;Clark,WP
通讯作者:
Clark,WP
DOI:
--
发表时间:
1983
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Aris,JP;Simoni,RD
通讯作者:
Simoni,RD
DOI:
--
发表时间:
1990
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Uh,M;Jones,D;Mueller,DM
通讯作者:
Mueller,DM