Cloning and Characterization of NAD-dependent Deacetylase Sirtuin 2 Homolog from the Silkworm, Bombyx mori.

Yijia Li, Keping Chen, Qin Yao, Lu Gao, Jun Li, Lin Wang


Sirtuin2 (Sirt2) is a kind of NAD+-dependent deacetylases ranging from bacteria to human and play an important role in
many biological processes especially in lifespan. We performed genome analysis and protein prediction of Sirt2 of B.
mori (BmSirt2). The cDNA sequence of BmSirt2 contains an ORF of 1164 bp encoding 387 amino acid residues with a
predicted molecular mass and isoelectric point of 43.37 kDa and 5.02, respectively. This protein shows high degrees of
identity with other species. Phylogenetic relationship analysis showed that the BmSirt2 protein was in the same
subgroup as the Sirt2 from invertebrate animals. RT-PCR analysis of gene expression in multiple tissues showed that
Sirt2 gene was widely expressed in B. mori. BmSirt2 was successfully expressed in E. coli with a molecular mass of
48.0 kDa. The identification of the recombinant protein by MALDI-TOF-MS and western blotting showed this fusion
protein was the correct one.

Full Text:



International Journal of Biology   ISSN 1916-9671(Print)   ISSN 1916-968X  (Online)

Copyright © Canadian Center of Science and Education

To make sure that you can receive messages from us, please add the '' domain to your e-mail 'safe list'. If you do not receive e-mail in your 'inbox', check your 'bulk mail' or 'junk mail' folders.


scholar_logo_lg_2011_120 proquest_logo_120 lockss_logo_2_120