Search results for "Mating of yeast"

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Regulation of mating in the budding yeast Saccharomyces cerevisiae by the zinc cluster proteins Sut1 and Sut2

2013

This article is made available through the Brunel Open Access Publishing Fund. Copyright @ The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The zinc cluster proteins Sut1 and Sut2 play a role in sterol uptake and filamentous growth in the budding yeast Saccharomyces cerevisiae. In this study, we show that they are also involved in mating. Cells that lack both SUT1 and SUT2 were defective in mating. The expression of the genes NCE102 and PRR2 was increased in the sut1 sut2 double deletion mutant…

Saccharomyces cerevisiae ProteinsMonosaccharide Transport ProteinsSaccharomyces cerevisiaeBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryFungal ProteinsGene Expression Regulation FungalReproduction AsexualBudding yeastMatingMolecular BiologyGenereproductive and urinary physiologyGeneticsMatingZinc FingersCell Biologybiology.organism_classificationBudding yeastSut2Sut1Mating of yeastPheromone responseZinc cluster proteinsZinc Clusterbehavior and behavior mechanismsPheromoneTranscription FactorsSterol uptakeBiochemical and Biophysical Research Communications
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Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae

2014

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during …

TranslationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalForminsRNA-binding proteinSaccharomyces cerevisiaeInvestigationsPeptide Initiation FactorsMorphogenesisGeneticsQc-SNARE ProteinsPolyproline helixPolarisomeGeneticsMatingbiologyMicrofilament ProteinsMembrane ProteinsRNA-Binding ProteinsTranslation (biology)Polarized growthbiology.organism_classificationActinsProtein Structure TertiaryCell biologyCytoskeletal ProteinsMating of yeastForminsMutationbiology.proteinEIF5APeptidesRibosomesEIF5A
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