Cloning of monoacylglycerol o-acyltransferase 2 cDNA from a silkworm, Bombyx mori

Abstract

Monoacylglycerol O-acyltransferase 2 (MOGAT2) plays critical roles in lipid homeostasis. We reported a cDNA designed BmMOGAT2 encoding an MOGAT2 homologue cloned from the fat body of the silkworm Bombyx mori, by using conserved domain homology search method. The resultant BmMOGAT2 was translated to a protein encoding 352 amino acids with a theoretical isoelectric point of 9.04 and a molecular weight of 39,944.48 Da. Homology analysis revealed that BmMOGAT2 exhibits higher similarity on the amino acid level to those of other species already reported; 48% identity with Homo sapiens, 46% with Mus musculus, 50% with Danio rerio, and 42% with Drosophila melanogaster. The expression of BmMOGAT2 was detected in all tissues tested with 2-fold higher expression in the post-silk gland, as compared to others, and stronger expression of the larval fat body at 1st instar, as compared with other stages. The BmMOGAT2 is a predicted endoplasmic reticulum (ER) transmembrane protein with two ER transmembrane domains; BmMOGAT2 gene expression increases in response to ER stress-inducible drugs. To our knowledge, this is the first report of Bombyx mori MOGAT2 cDNA, BmMOGAT2, and its associated molecular characterization.