Cloning of monoacylglycerol o-acyltransferase 2 cDNA from a silkworm, Bombyx mori
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Hyojung Shin
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.
Acknowledgements
This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2013R1A1A 2064049).
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- Abbreviations
- BmMOGAT2
Bombyx mori MOGAT2 cDNA
- DAG
diacylglycerol
- DD-PCR
differential display PCR
- ER
endoplasmic reticulum
- MAG
monoacylglycerol
- MGAT
O-acyltransferase
- MOGAT2
monoacylglycerol O-acyltransferase2
- RT-PCR
reverse transcriptional PCR
- TG
triacylglycerol
- VLDL
very low-density lipoprotein.
©2016 Institute of Molecular Biology, Slovak Academy of Sciences
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- Botany
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