[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

A soluble diacylglycerol acyltransferase is involved in triacylglycerol biosynthesis in the oleaginous yeast Rhodotorula glutinis.

Sapa, Hima Rani and Saha, Saikat and Ram, Rajasekharan (2013) A soluble diacylglycerol acyltransferase is involved in triacylglycerol biosynthesis in the oleaginous yeast Rhodotorula glutinis. Microbiology, 159. pp. 155-166.

[img] PDF
Micrbiol Reprint.pdf - Published Version
Restricted to Registered users only

Download (526kB) | Request a copy

Abstract

The biosynthesis of triacylglycerol (TAG) occurs in the microsomal membranes of eukaryotes. Here, we report the identification and functional characterization of diacylglycerol acyltransferase (DGAT), a member of the 10 S cytosolic TAG biosynthetic complex (TBC) in Rhodotorula glutinis. Both a full-length and an N-terminally truncated cDNA clone of a single gene were isolated from R. glutinis. The DGAT activity of the protein encoded by RgDGAT was confirmed in vivo by the heterologous expression of cDNA in a Saccharomyces cerevisiae quadruple mutant (H1246) that is defective in TAG synthesis. RgDGAT overexpression in yeast was found to be capable of acylating diacylglycerol (DAG) in an acyl-CoA-dependent manner. Quadruple mutant yeast cells exhibit growth defects in the presence of oleic acid, but wild-type yeast cells do not. In an in vivo fatty acid supplementation experiment, RgDGAT expression rescued quadruple mutant growth in an oleate-containing medium. We describe a soluble acyl-CoA-dependent DAG acyltransferase from R. glutinis that belongs to the DGAT3 class of enzymes. The study highlights the importance of an alternative TAG biosynthetic pathway in oleaginous yeasts.

Item Type: Article
Uncontrolled Keywords: Rhodotorula glutinis, diacylglycerol acyltransferase, biosynthesis
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 19 Yeast
Divisions: Director's Office
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 26 Dec 2012 11:15
Last Modified: 26 Dec 2012 11:15
URI: http://ir.cftri.com/id/eprint/11071

Actions (login required)

View Item View Item