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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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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:
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
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author de Kok, Stefan
Yilmaz, Duygu
Daran, Jean-Marc
Pronk, Jack T.
van Maris, Antonius J. A.
author_facet de Kok, Stefan
Yilmaz, Duygu
Daran, Jean-Marc
Pronk, Jack T.
van Maris, Antonius J. A.
author_sort de Kok, Stefan
collection PubMed
description 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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spelling pubmed-33972122012-07-23 In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry de Kok, Stefan Yilmaz, Duygu Daran, Jean-Marc Pronk, Jack T. van Maris, Antonius J. A. Antonie Van Leeuwenhoek Short Communication 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. Springer Netherlands 2012-04-10 2012 /pmc/articles/PMC3397212/ /pubmed/22488179 http://dx.doi.org/10.1007/s10482-012-9730-2 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Short Communication
de Kok, Stefan
Yilmaz, Duygu
Daran, Jean-Marc
Pronk, Jack T.
van Maris, Antonius J. A.
In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title_full In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title_fullStr In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title_full_unstemmed In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title_short In vivo analysis of Saccharomyces cerevisiae plasma membrane ATPase Pma1p isoforms with increased in vitro H(+)/ATP stoichiometry
title_sort in vivo analysis of saccharomyces cerevisiae plasma membrane atpase pma1p isoforms with increased in vitro h(+)/atp stoichiometry
topic Short Communication
url 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
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