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Linking post-translational modifications and variation of phenotypic traits.
Mol Cell Proteomics ; 12(3): 720-35, 2013 Mar.
Article em En | MEDLINE | ID: mdl-23271801
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Variação Genética / Processamento de Proteína Pós-Traducional Limite: Humans Idioma: En Revista: Mol Cell Proteomics Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: França

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Variação Genética / Processamento de Proteína Pós-Traducional Limite: Humans Idioma: En Revista: Mol Cell Proteomics Assunto da revista: BIOLOGIA MOLECULAR / BIOQUIMICA Ano de publicação: 2013 Tipo de documento: Article País de afiliação: França