4.3 Article

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

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SPRINGER
DOI: 10.1007/s10482-012-9730-2

Keywords

Pma1; Ser800Ala; Glu803Gln; Maltose; Yeast; Proton symport

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Funding

  1. Tate & Lyle Ingredients Americas Inc.
  2. Netherlands Genomics Initiative

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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.

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