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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Complementation in situ of the yeast plasma membrane H(+)-ATPase gene pma1 by an H(+)-ATPase gene from a heterologous species.

In plants and fungi, the transport of solutes across the plasma membrane (pm) is driven by a proton pump (H(+)-ATPase) that produces an electric potential and a pH gradient. We expressed AHA2, a member of the Arabidopsis thaliana pm H(+)-ATPase gene family, in yeast cells in which transcription of the endogenous pm H(+)-ATPase gene (pma1) had been turned off. AHA2 was expressed mainly in intracellular membranes and only supported very slow growth of transformed yeast cells. Removal of the last 92 C-terminal amino acids from the plant H(+)-ATPase produced an enzyme with 2-3-fold higher specific ATPase activity than the wild-type plant enzyme. Surprisingly, the truncated H(+)-ATPase was now targetted to the yeast pm and fully supported normal yeast growth.[1]

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