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

Hiroshi Yamada, Yoshinori Moriyama, Masatomo Maeda, Masamitsu Futai

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)34-38
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - Jul 15 1996
Externally publishedYes


  • ATP synthase
  • H-ATPase
  • Hydrophobic F subunit
  • Subunit a

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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