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

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Title
Cloning of monoacylglycerol o-acyltransferase 2 cDNA from a silkworm, Bombyx mori
Author(s)
H Shin; K Kwon; S M Hong; H G Kim; J Y Choi; S W Kim; Kweon Yu; O Y Kwon
Bibliographic Citation
Biologia, vol. 71, no. 6, pp. 695-700
Publication Year
2016
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.
Keyword
BmMOGAT2Bombyx morimonoacylglycerol O-acyltransferase 2silkworm
ISSN
0006-3088
Publisher
Springer
DOI
http://dx.doi.org/10.1515/biolog-2016-0090
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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