Abstract
Plasma membrane H+-ATPase isoforms with increased H+/ATP ratios represent a desirable asset in yeast metabolic engineering. In vivo proton coupling of two previously reported Pma1p isoforms (Ser800Ala, Glu803Gln) with increased in vitro H+/ATP stoichiometries was analysed by measuring biomass yields of anaerobic maltose-limited chemostat cultures expressing only the different PMA1 alleles. In vivo H+/ATP stoichiometries of wildtype Pma1p and the two isoforms did not differ significantly.
Highlights
Plasma membrane H?-ATPases are ubiquitous enzymes that play an important role in eukaryotic physiology by using the free energy from ATP hydrolysis to pump protons from the cytosol, across the plasma membrane and out of the cell
In vivo proton coupling of two previously reported Pma1p isoforms (Ser800Ala, Glu803Gln) with increased in vitro H?/ ATP stoichiometries was analysed by measuring biomass yields of anaerobic maltose-limited chemostat cultures expressing only the different PMA1 alleles
The present study investigates whether the in vivo H?/ ATP stoichiometry of S. cerevisiae Pma1p isoforms can be analysed via the anaerobic biomass yield on maltose of engineered strains
Summary
Stefan de Kok • Duygu Yilmaz • Jean-Marc Daran • Jack T. Pronk • Antonius J. A. van Maris Received: 19 January 2012 / Accepted: 22 March 2012 / Published online: 10 April 2012 Ó The Author(s) 2012. This article is published with open access at Springerlink.com
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