GCN5 Gene Product Essential for Transcriptional Regulation of TPS1 and NTH1 Genes

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Turgut Genç T., Toyran G.

Anatolian 8th International Applied Sciences Congress, Diyarbakır, Turkey, 25 - 26 December 2021, pp.30-31

  • Publication Type: Conference Paper / Summary Text
  • City: Diyarbakır
  • Country: Turkey
  • Page Numbers: pp.30-31
  • Çanakkale Onsekiz Mart University Affiliated: Yes


Trehalose is a highly stable, non-reducing disaccharide found in many organisms. Trehalose acts as an energy source and stress-protecting molecule in yeast cells. Trehalose is accumulated as a stress response under various stress conditions. The trehalose content of cells is regulated by trehalose synthesis and degradation enzymes. Trehalose is synthesized by the TPS complex including Tps1p Tps2, Tps3 and Tsl1 proteins, and stress-accumulated trehalose is degraded by the neutral trehalase enzyme, Nth1p. TPS1 and NTH1 genes are multiple stress response genes and their expressions are regulated by different mechanisms. Histone acetylation (HAT) and deacetylation (HDA) are important epigenetic mechanisms for transcriptional activation in response to physiological changes and various stresses. SAGA (Spt-Ada-Gcn5 acetyltransferase) is a transcription coactivator complex that controls the transcription by modifying chromatin structure. Gcn5 is a transcriptional regulatory protein containing histone acetyltransferase activity. It has been shown that promoter acetylation and transcriptional activation in the trehalose metabolic pathway are increased in the absence of HDA. In our study, it was aimed to determine the effect of Gcn5 protein on TPS1 and NTH1 gene expressions using Δgcn5 mutant and wild type yeast strains. The promoter activities of TPS1 and NTH1 increased 5-fold and 14-fold in ∆gcn5 yeast strains respectively, under normal growth conditions. However, the TPS1 promoter activity of mutant yeast cells was 3 times lower than that of the wild type strain in the stress condition.