期刊
MOLECULES
卷 26, 期 18, 页码 -出版社
MDPI
DOI: 10.3390/molecules26185470
关键词
Saccharomyces cerevisiae; Pah1 phosphatidate phosphatase; N-terminal Lipin (NLIP) domain; C-terminal Lipin (CLIP); haloacid dehalogenase (HAD)-like domain; Lipin 1 phosphatidate phosphatase; thioredoxin
资金
- Ministry of Science and Technology, Taiwan [MOST 108-2320-B-029-001-]
This study investigated the relationship between the catalytic activity of Pah1 and Lipin 1 and their structural domains, revealing that the conserved N- and C-terminal domains are essential for the activity of Pah1. Removal of disordered hydrophilic regions significantly reduced the protein solubility of Pah1.
Saccharomyces cerevisiae Pah1 phosphatidate phosphatase (PAP) catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol, controlling phospholipids and triacylglycerol metabolisms. Pah1 and human Lipin 1 are intrinsically disordered proteins with 56% and 43% unfolded regions, respectively. Truncation analysis of the conserved and non-conserved regions showed that N- and C-conserved regions are essential for the catalytic activity of Pah1. PAP activities can be detected in the conserved N-terminal Lipin (NLIP) domain and C-terminal Lipin (CLIP)/haloacid dehalogenase (HAD)-like domain of Pah1 and Lipin 1, suggesting that the evolutionarily conserved domains are essential for the catalytic activity. The removal of disordered hydrophilic regions drastically reduced the protein solubility of Pah1. Thioredoxin is an efficient fusion protein for production of soluble NLIP-HAD recombinant proteins in Escherichia coli.
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