Transmembrane topology of Escherichia coli H+-ATPase (ATP synthase) subunit a

被引：29

作者：

Yamada, H ^{[1
]}

Moriyama, Y ^{[1
]}

Maeda, M ^{[1
]}

Futai, M ^{[1
]}

机构：

[1] OSAKA UNIV,INST SCI & IND RES,DEPT BIOL SCI,IBARAKI,OSAKA 567,JAPAN

来源：

FEBS LETTERS | 1996年 / 390卷 / 01期

关键词：

H+-ATPase; ATP synthase; subunit a; hydrophobic F-0 subunit;

D O I：

10.1016/0014-5793(96)00621-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Escherichia coli H+-ATPase subunit alpha is a hydrophobic F-0 subunit. To investigate the topology of the subunit in the membrane, we prepared site-specific polyclonal antibodies against amino-terminal (Ser3 to Leu-16), middle loop (Lys-167 to Gln-181), and carboxyl-terminal (Thr-259 to His-271) peptide segments. Enzyme-linked immunosorberat assay revealed that these antibodies specifically reacted with subunit a of inside-out membrane vesicles, but not with that of Fight-side-out spheroplasts. Full reactivity appeared when spheroplasts were disrupted with Triton X-100 (0.5%) or by sonication. These results suggest that at least parts of the three peptide-segments of subunit a face the cytoplasm, Based on these observations, we propose a novel transmembrane topology of subunit a.

引用

页码：34 / 38

页数：5