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Title
Interfering with glycolysis causes Sir2-dependent hyper-recombination of Saccharomyces cerevisiae plasmids
AuthorRalser, Markus ; Zeidler, Ute ; Lehrach, Hans
Published in
PLoS ONE, Lawrence, Kan., 2009, Vol. 4, page 1-9
PublishedPublic Library of Science, 2009
LanguageEnglish
Document typeJournal Article
Keywords (EN)Plasmid construction / Saccharomyces cerevisiae / Yeast / Recombination-based assay / Enzyme metabolism / Glycolysis / Transformation associated recombination / Cloning
ISSN1932-6203
URNurn:nbn:at:at-ubs:3-6012 Persistent Identifier (URN)
DOI10.1371/journal.pone.0005376 
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 The work is publicly available
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Interfering with glycolysis causes Sir2-dependent hyper-recombination of Saccharomyces cerevisiae plasmids [0.88 mb]
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Abstract (English)

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key metabolic regulator implicated in a variety of cellular processes. It functions as a glycolytic enzyme, a protein kinase, and a metabolic switch under oxidative stress. Its enzymatic inactivation causes a major shift in the primary carbohydrate flux. Furthermore, the protein is implicated in regulating transcription, ER-to-Golgi transport, and apoptosis. We found that Saccharomyces cerevisiae cells null for all GAPDH paralogues (Tdh1, Tdh2, and Tdh3) survived the counter-selection of a GAPDHencoding plasmid when the NAD+ metabolizing deacetylase Sir2 was overexpressed. This phenotype required a fully functional copy of SIR2 and resulted from hyper-recombination between S. cerevisiae plasmids. In the wild-type background, GAPDH overexpression increased the plasmid recombination rate in a growth-condition dependent manner. We conclude that GAPDH influences yeast episome stability via Sir2 and propose a model for the interplay of Sir2, GAPDH, and the glycolytic flux.

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