PMID:9518621
| Citation |
Hatch, LP, Cox, GB and Howitt, SM (1998) Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent. Biochim. Biophys. Acta 1363:217-23 |
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| Abstract |
The role of glutamate-219 in the a-subunit of the Escherichia coli F0F1-ATPase was examined using site-directed mutagenesis. The replacement of Glu-219 by lysine, alanine or glycine resulted in a partially functional F0F1-ATPase. Combining any of these mutations with the substitution of glutamate for Gln-252 did not result in any increase in function. These findings rule out a proposal that glutamate at position 252 can functionally replace glutamate at position 219 [S.B. Vik, B.J. Antonio, J. Biol. Chem. 269 (1994) 30364-30369]. All the single and double mutants grew better at 25 degrees C than at 37 degrees C, suggesting a role for Glu-219 in maintaining the structure of the F0. |
| Links | |
| Keywords |
Cell Membrane/enzymology; Computer Simulation; Escherichia coli/enzymology; Escherichia coli/genetics; Glutamic Acid/analysis; Glutamic Acid/metabolism; Mutagenesis, Site-Directed; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/genetics; Proton-Translocating ATPases/metabolism |
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