Bg. Bhat et al., Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein, BBA-MOL C B, 1439(3), 1999, pp. 415-423
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
Rat mitochondrial glycerol-3-phosphate acyltransferase (GPAT) cDNA was clon
ed and characterized. We identified a cDNA containing an open reading frame
of 828 amino acids that had an 89% homology with the coding region of the
previously characterized mouse mitochondrial GPAT and a predicted amino aci
d sequence that was 96% identical. The rat 5' UTR was only 159 nucleotides,
in contrast to the 926 nucleotide 5' UTR of the mouse cDNA and had an inte
rnal deletion of 167 nucleotides. GPAT was expressed in Sf21 insect cells,
and specific inhibitors strongly suggest that, like the Escherichia coli GP
AT, the recombinant mitochondrial GPAT and the mitochondrial GPAT isoform i
n rat liver contain critical serine, histidine, and arginine residues. (C)
1999 Elsevier Science B.V. All rights reserved.