| Literature DB >> 23271801 |
Warren Albertin1, Philippe Marullo, Marina Bely, Michel Aigle, Aurélie Bourgais, Olivier Langella, Thierry Balliau, Didier Chevret, Benoît Valot, Telma da Silva, Christine Dillmann, Dominique de Vienne, Delphine Sicard.
Abstract
Enzymes can be post-translationally modified, leading to isoforms with different properties. The phenotypic consequences of the quantitative variability of isoforms have never been studied. We used quantitative proteomics to dissect the relationships between the abundances of the enzymes and isoforms of alcoholic fermentation, metabolic traits, and growth-related traits in Saccharomyces cerevisiae. Although the enzymatic pool allocated to the fermentation proteome was constant over the culture media and the strains considered, there was variation in abundance of individual enzymes and sometimes much more of their isoforms, which suggests the existence of selective constraints on total protein abundance and trade-offs between isoforms. Variations in abundance of some isoforms were significantly associated to metabolic traits and growth-related traits. In particular, cell size and maximum population size were highly correlated to the degree of N-terminal acetylation of the alcohol dehydrogenase. The fermentation proteome was found to be shaped by human selection, through the differential targeting of a few isoforms for each food-processing origin of strains. These results highlight the importance of post-translational modifications in the diversity of metabolic and life-history traits.Entities:
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Year: 2012 PMID: 23271801 PMCID: PMC3591664 DOI: 10.1074/mcp.M112.024349
Source DB: PubMed Journal: Mol Cell Proteomics ISSN: 1535-9476 Impact factor: 5.911