Role of minor subunits in the structural asymmetry of the Escherichia coli F1-ATPase.
The beta subunits of the Escherichia coli F1-ATPase react independently with chemical reagents (Stan-Lotter, H. and Bragg, P.D. (1986) Arch. Biochem. Biophys. 248, 116-120). Thus, one beta subunit is readily crosslinked to the epsilon subunit, another reacts with N-N'-dicyclohexylcarbodiimide (DCCD), and a third one is modified by 4-chloro-7-nitrobenzofurazan (NbfCl). This asymmetric behaviour is not due to the association of the delta and epsilon subunits of the ATPase molecule with specific beta subunits since it is maintained in a delta, epsilon-deficient form of the enzyme.
Bragg
P D
PD
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
Hou
C
C
D001572:Benzofurans / Q000378:metabolism; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009154:Mutation; D009282:Naphthalenesulfonates; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D014357:Trypsin
D001572:Benzofurans; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009282:Naphthalenesulfonates; D004024:Dicyclohexylcarbodiimide; C011488:IAANS; C059027:4-chloro-7-nitrobenzofuran; D014357:Trypsin; D006180:Proton-Translocating ATPases