Crystal structure of the complex of DNA with the C-terminal domain of TYE7 from Saccharomyces cerevisiae

Abstract

TYE7, a bHLH (basic helix–loop–helix) transcription factor from Saccharomyces cerevisiae, is involved in the regulation of many genes, including glycolytic genes. Meanwhile, accumulating evidence indicates that TYE7 also functions as a cyclin and is linked to sulfur metabolism. Here, the structure of TYE7 (residues 165–291) complexed with its specific DNA was determined by X-ray crystallography. Structural analysis and comparison revealed that His185 and Glu189 are conserved in base recognition. However, Arg193 is also involved in base recognition in the structures that were compared. In the structure in this study, Arg193 in chain A has two conformations and makes a salt bridge with the phosphate backbone structure. In addition, a series of corresponding electrophoretic mobility shift assays were performed to better understand the DNA-binding mechanism of the bHLH domain of TYE7.

Regulatory mechanism of Haa1p and Tye7p in Saccharomyces cerevisiae when fermenting mixed glucose and xylose with or without inhibitors

“…For all the target genes regulated by these potential TFs, only 2 genes in 336 genes regulated by Met32p were DEGs in C_T vs. C_S group. This indicated that the regulatory mechanisms of Tye7p and its regulated TFs during mixed sugar fermentation were possibly very different from those with the fermentation of glucose under the conditions of most researchers studied [ 34 , 35 ]. Hence, further studies are needed to reveal the genes they regulate and the contributions of these TFs to xylose metabolism and inhibitor tolerance.…”

“…Tye7p, a transcriptional activator, contributes to glycolytic genes activation, such as ENO1 and ENO2 (enolase), TDH (glyceraldehyde-3-phosphate dehydrogenase), PGK1 (phosphoglycerate kinase), PGM1 (phosphoglycerate mutase), PYK1 (pyruvate kinase), and TPI1 (triosephosphate isomerase) [ 32 , 33 ]. Researchers have revealed that Tye7p involves in the positive regulation of the glycolytic process and activates Ty1 mRNA transcription [ 34 , 35 ]. However, the regulation mechanism of Tye7p in response to inhibitors has not been reported.…”