A novel human glycosyltransferase:: primary structure and characterization of the gene and transcripts

被引:19
作者
Heinonen, TYK [1 ]
Pasternack, L
Lindfors, K
Breton, C
Gastinel, LN
Mäki, M
Kainulainen, H
机构
[1] Tampere Univ, Sch Med, Paediat Res Ctr, FIN-33101 Tampere, Finland
[2] Tampere Univ Hosp, Tampere, Finland
[3] Univ Grenoble 1, CNRS, Ctr Rech Macromol Vegetales, Grenoble, France
[4] Univ Limoges, Inst Sci Vie & Sante, EA Glycobiol Vegetale & Biotechnol 3176, Limoges, France
[5] Tampere Univ, Inst Med Technol, FIN-33101 Tampere, Finland
关键词
glycosyltransferase; catalytic domain; cDNA clone; gene organization;
D O I
10.1016/S0006-291X(03)01540-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We report the identification and primary structure of a novel human glycosyltransferase, B3GTL (beta3-glycosyltransferase-like). The 498 residue protein consists of a short cytoplasmic N-terminal "tail" (residues 1-4), a single transmembrane domain with type II topology (residues 5-28), a "stem" region (residues 29-260), and a catalytic domain (residues 261-498). The genomes of Anopheles gambiae, Drosophila melanogaster, and Caenorhabditis elegans encode potential orthologs which share 31-39% sequence identity with B3GTL, as well as the following features: a conserved catalytic domain containing a triple aspartate motif (DDD) at its core, a conserved pattern of cysteine residues, a C-terminal KDEL-like motif, and conserved residues and motifs that affiliate this novel group with a family of beta3-glycosyltransferases (GT31 in the CAZY classification). The B3GTL gene lacks canonical TATA and CAAT boxes and contains three functional polyadenylation sites. It is transcribed in a wide range of tissues and in TGF-beta-treated T84 epithelial cells. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:166 / 174
页数:9
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