ISOLAMENTO E CARACTERIZAÇÃO DE UM MUTANTE DE Saccharomyces cerevisiae COM CARACTERÍSTICAS FENOTÍPICAS OPOSTAS À CEPA pkcΔ

AUTOR(ES)
FONTE

IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia

DATA DE PUBLICAÇÃO

16/06/2004

RESUMO

It is known that in yeast, protein kinase C participates in the regulation of the biochemical pathway responsible for the transcription of the glucano-synthase enzyme subunits, which is involved in cell wall synthesis. The PKC MAP kinase pathway consists of Bck1, Mkk1/2 and Mpk1 enzymes that are activated by phosphorylation. Recently, we discovered that pkc1Δ mutant, as opposite to mutants in the MAP kinase cascade, displays two major defects in the control of carbon metabolism. It shows a delay in the initiation of fermentation and a defect in derepression after exhaustion of glucose of the medium. These factors are consistent with the hypothesis that there is a bifurcation after PKC, suggesting that this protein kinase has several important functions in yeast. Based on the characteristic that pkc1Δ mutant is unable to grow on glycerol, we isolated a new mutant from pkc1Δ strain that presented normal grow on glycerol. The new mutant (LBFM 335) was transformed with a yeast genomic DNA library and we isolated two transformants (LBFM 342 and LBFM 345) that recovered the original phenotype of pkc1Δ mutant (unable to grow on glycerol). In this work, we characterized a new mutant (LBFM335) that relieves the pkc1Δ repressive phenotype in Saccharomyce cerevisiae. Furthermore, we isolated two extragenic suppressors of this mutation that were identified as the Nuclear Exportin Msn5 and the Histone Deacetylase Hos2.

ASSUNTO(S)

saccharomyces cerevisiae cepa pkcΔ mutante biologia molecular

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