Aerobic Growth of Escherichia coli Is Reduced and ATP Synthesis Is Selectively Inhibited When Five C-Terminal Residues Are Deleted from the ε Subunit of ATP Synthase

Shah N, Duncan T, 290(34):21032-41, J Biol Chem , 2015

This study suggests that in different bacterial species the C-terminal domain of ε-subunit (εCTD) of ATP synthase could be fine-tuned to regulate ATP synthesis as well as ATP hydrolysis. The study also found that such regulation of functions is based on the unique metabolic and environmental demands of each bacterial species. A variety of molecular biology approaches including mutagenesis, phenotyping, expression, and purification of enzymes were used in this investigation. The interaction between F1(-σε) and biotinylated ε variants were estimated by an Octet RED system equipped with Streptavidin Biosensor probes. The dissociation phase in each interaction was analyzed to obtain the off-rates using nonlinear regression fits for two phases of exponential decay.

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