Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 278, Issue 18, Pages 15571-15578Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M301123200
Keywords
-
Categories
Funding
- NICHD NIH HHS [R01 HD042769] Funding Source: Medline
Ask authors/readers for more resources
Heparan and chondroitin sulfates play essential roles in growth factor signaling during development and share a common linkage tetrasaccharide structure, GlcAbeta1,3Galbeta1,3Galbeta1,4Xylbeta1-O-Ser. In the present study, we identified the Drosophila proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I (dbeta4GalTI), and determined its substrate specificity. The enzyme transferred a Gal to the -beta-xylose (XyI) residue, confirming it to be the Drosophila ortholog of human proteoglycan UDP-galactose:beta-xylose 01,4-galactosyltransferase I. Then we established UAS-dbeta4GalTI-IR fly lines containing an inverted repeat of dbeta4GalTI ligated to the upstream activating sequence (UAS) promoter, a target of GAL4, and observed the Fi(1) generation of the cross between the UAS-dbeta4GalTI-IR fly and the Act5C-GAL4 fly. In the F, double-stranded RNA of dbeta4GalTI is expressed ubiquitously under the control of a cytoplasmic actin promoter to induce the silencing of the dbeta4GalTI gene. The expression of the target gene was disrupted specifically, and the degree of interference was correlated with phenotype. The lethality among the progeny proved that beta4GalTI is essential for viability. This study is the first to use reverse genetics, RNA interference, to study the Drosophila glycosyltransferase systematically.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available