The abundance of atp gene transcript and of the membrane F1F0-ATPase as a function of the growth pH of alkaliphilic Bacillus firmus OF4.
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.
Ivey
D M
DM
Department of Biochemistry, Mount Sinai School of Medicine of City University of New York, New York 10029.
Sturr
M G
MG
Krulwich
T A
TA
Hicks
D B
DB
D001407:Bacillus / Q000201:enzymology / Q000235:genetics*; D015153:Blotting, Western; D002462:Cell Membrane / Q000201:enzymology; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D009876:Operon; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism; D012329:RNA, Bacterial / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics
D012329:RNA, Bacterial; D012333:RNA, Messenger; D006180:Proton-Translocating ATPases