The abundance of atp gene transcript and of the membrane F1F0-ATPase as a function of the growth pH of alkaliphilic Bacillus firmus OF4

J Bacteriol. 1994 Aug;176(16):5167-70. doi: 10.1128/jb.176.16.5167-5170.1994.

Abstract

Molecular biological and biochemical studies of the F(1)F(0)-ATP synthase of alkaliphilic Bacillus firmus OF4 show that the enzyme used at pH 7.5 and pH 10.5 is a unique product of the atp operon, expressed at the same levels and yielding an enzyme with the same subunit properties and c-subunit/holoenzyme stoichiometry.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus / enzymology
  • Bacillus / genetics*
  • Blotting, Western
  • Cell Membrane / enzymology
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Hydrogen-Ion Concentration
  • Operon
  • Proton-Translocating ATPases / genetics*
  • Proton-Translocating ATPases / metabolism
  • RNA, Bacterial / genetics
  • RNA, Messenger / genetics

Substances

  • RNA, Bacterial
  • RNA, Messenger
  • Proton-Translocating ATPases