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

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...

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Detalles Bibliográficos
Autores principales: de Kok, Stefan, Yilmaz, Duygu, Daran, Jean-Marc, Pronk, Jack T., van Maris, Antonius J. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2012
Materias:
Short Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3397212/
https://www.ncbi.nlm.nih.gov/pubmed/22488179
http://dx.doi.org/10.1007/s10482-012-9730-2
Descripción
Sumario: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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