화학공학소재연구정보센터
International Journal of Molecular Sciences, Vol.8, No.5, 433-444, 2007
Molecular cloning and characterization of a novel human glycine-N-acyltransferase gene GLYATL1, which activates transcriptional activity of HSE pathway
The glycine-N-acyltransferase (GLYAT) is well known to be involved in the detoxification of endogenous and exogenous xenobiotic acyl-CoA's in mammals. Unfortunately, the knowledge about the gene encoding GLYAT is very limited. Here we report a novel gene encoding a GLYAT member, designated as GLYATL1, which was 1546 base pairs in length and contained an open reading frame (ORF) encoding a polypeptide of 302 amino acids. GLYATL1 was a split gene that was consisted of 7 exons and 6 introns and mapped to chromosome 11q12.1. The expression of GLYATL1 could be found in liver, kidney, pancreas, testis, ovary and stomach among 18 human tissues by RTPCR analysis. Subcellular localization of myc-tagged GLYATL1 fusion protein revealed that GLYATL1 was distributed primarily in the cytoplasm of COS-7 cells. Furthermore, through the pathway profiling assay, the GLYATL1 protein was found to activate HSE signaling pathway in a dose-dependent manner when overexpressed in HEK293T cells.