1996年7月15日
Transmembrane topology of Escherichia coli H+-ATPase (ATP synthase) subunit a
FEBS Letters
- ,
- ,
- ,
- 巻
- 390
- 号
- 1
- 開始ページ
- 34
- 終了ページ
- 38
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/0014-5793(96)00621-7
- 出版者・発行元
- Elsevier B.V.
Escherichia coli H+-ATPase subunit a is a hydrophobic F0 subunit. To investigate the topology of the subunit in the membrane, we prepared site-specific polyclonal antibodies against amino-terminal (Ser-3 to Leu-16), middle loop (Lys-167 to Gln-181), and carboxyl-terminal (Thr-259 to His-271) peptide segments. Enzyme-linked immunosorbent assay revealed that these antibodies specifically reacted with subunit a of inside-out membrane vesicles, but not with that of right-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.
- リンク情報
- ID情報
-
- DOI : 10.1016/0014-5793(96)00621-7
- ISSN : 0014-5793
- PubMed ID : 8706824
- SCOPUS ID : 0030586274