Akademik Veri Yönetim Sistemi
Anatolian 8th International Applied Sciences Congress, Diyarbakır, Türkiye, 25 - 26 Aralık 2021, ss.30-31
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.