Glycolytic flux in Saccharomyces cerevisiae is dependent on RNA polymerase III and its negative regulator Maf1
Autor: | Malgorzata Adamczyk, Emil Furmanek, Stephen W. Holman, Roza Szatkowska, Simon J. Hubbard, Manuel Garcia-Albornoz, Robert J. Beynon, Katarzyna Roszkowska |
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Jazyk: | angličtina |
Rok vydání: | 2019 |
Předmět: |
chemistry.chemical_classification
0303 health sciences biology Chemistry Saccharomyces cerevisiae Mutant genetic processes Cell Biology Metabolism biology.organism_classification Biochemistry RNA polymerase III 03 medical and health sciences enzymes and coenzymes (carbohydrates) 0302 clinical medicine Enzyme Transcription (biology) Protein biosynthesis health occupations bacteria Molecular Biology Gene 030217 neurology & neurosurgery 030304 developmental biology |
Zdroj: | BIOCHEMICAL JOURNAL Szatkowska, R, Garcia-Albornoz, M, Roszkowska, K, Holman, S W, Furmanek, E, Hubbard, S J, Beynon, R J & Adamczyk, M 2019, ' Glycolytic flux in Saccharomyces cerevisiae is dependent on RNA polymerase III and its negative regulator Maf1 ', Biochemical Journal, vol. 476, no. 7, pp. 1053-1082 . https://doi.org/10.1042/BCJ20180701 |
Popis: | Protein biosynthesis is energetically costly, is tightly regulated and is coupled to stress conditions including glucose deprivation. RNA polymerase III (RNAP III)-driven transcription of tDNA genes for production of tRNAs is a key element in efficient protein biosynthesis. Here we present an analysis of the effects of altered RNAP III activity on the Saccharomyces cerevisiae proteome and metabolism under glucose-rich conditions. We show for the first time that RNAP III is tightly coupled to the glycolytic system at the molecular systems level. Decreased RNAP III activity or the absence of the RNAP III negative regulator, Maf1 elicit broad changes in the abundance profiles of enzymes engaged in fundamental metabolism in S. cerevisiae. In a mutant compromised in RNAP III activity, there is a repartitioning towards amino acids synthesis de novo at the expense of glycolytic throughput. Conversely, cells lacking Maf1 protein have greater potential for glycolytic flux. |
Databáze: | OpenAIRE |
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