Protein Structure and Regulation of the TPS1 Gene of Yarrowia lipolytica

Abstract

Microbial thermostability is fundamental in biotechnology, as high temperatures reduce cell growth and metabolic efficiency. Yarrowia lipolytica is a yeast of biotechnological interest due to its ability to produce metabolites of industrial value; however, its growth is limited at temperatures above 32 °C. In response to stress, Y. lipolytica accumulates trehalose, a protective disaccharide synthesized by trehalose-6-phosphate synthase (TPS1). Understanding the structure and regulation of the TPS1 gene provides insight into elements associated with high temperature tolerance, which are key for genetic engineering strategies. The bioinformatic analysis of the TPS1 gene and protein in Y. lipolytica revealed a simple organization without introns and transcriptional regulation dependent on stressrelated cis-motifs, including HSE, STRE, GC-box, and TATA box. The tertiary structure showed high conservation of essential catalytic domains, including GT-20, DXD, and HXH, and of key residues, confirming its central role in trehalose synthesis and the importance of the active site for catalysis, stability, and thermal stress tolerance. We conclude that the TPS1 gene of Y. lipolytica is distinguished by its structural and regulatory efficiency under heat stress.