Short Communication

Antonie van Leeuwenhoek

, Volume 102, Issue 2, pp 401-406

First online:

Open Access This content is freely available online to anyone, anywhere at any time.

In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H+/ATP stoichiometry

  • Stefan de KokAffiliated withDepartment of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation
  • , Duygu YilmazAffiliated withDepartment of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation
  • , Jean-Marc DaranAffiliated withDepartment of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation
  • , Jack T. PronkAffiliated withDepartment of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation
  • , Antonius J. A. van MarisAffiliated withDepartment of Biotechnology, Delft University of Technology and Kluyver Centre for Genomics of Industrial Fermentation Email author 

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.

Keywords

Pma1 Ser800Ala Glu803Gln Maltose Yeast Proton symport