The chloroplast beta-subunit allows assembly of the Escherichia coli F0 portion of the energy transducing adenosine triphosphatase.
The effect of the expression of the chloroplast F1-ATPase beta-subunit in two Escherichia coli beta-subunit mutant strains was investigated. The amount of chloroplast beta-subunit formed in E. coli was increased by introducing a 'Shine-Dalgarno' sequence upstream from the translation start site. The chloroplast beta-subunit was membrane bound but was unable to functionally replace the mutant beta-subunit in a strain carrying the uncD409 allele [corrected]. However, in an E. coli mutant strain unable to form the beta- and epsilon-subunits the presence of the chloroplast beta-subunit enabled the assembly of a functional proton pore [corrected]
Munn
A L
AL
Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra City.
Whitfeld
P R
PR
Bottomley
W
W
Hudson
G S
GS
Jans
D A
DA
Gibson
F
F
Cox
G B
GB
D001483:Base Sequence; D002736:Chloroplasts / Q000201:enzymology*; D003001:Cloning, Molecular; D004247:DNA; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009154:Mutation; D010944:Plants / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism
D004247:DNA; D006180:Proton-Translocating ATPases