Document Detail


Molecular cloning and characterization of a novel alpha 1,2-fucosyltransferase (CE2FT-1) from Caenorhabditis elegans.
MedLine Citation:
PMID:  12163507     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Here we report the discovery of a unique fucosyltransferase (FT) in Caenorhabditis elegans. In studying the activities of FTs in extracts of adult C. elegans, we detected activity toward the unusual disaccharide acceptors Galbeta1-4Xyl-R and Galbeta1-6GlcNAc-R to generate products with the general structure Fucalpha1-2Galbeta1-R. We identified a gene encoding a unique alpha1,2FT (designated CE2FT-1), which contains an open reading frame encoding a predicted protein of 355 amino acids with the type 2 topology and domain structure typical of other glycosyltransferases. The predicted cDNA for CE2FT-1 has very low identity (5-10%) at the amino acid level to alpha1,2FT sequences in humans, rabbits, and mice. Recombinant CE2FT-1 expressed in human 293T cells has high alpha1,2FT activity toward the simple acceptor Galbeta-O-phenyl acceptor to generate Fucalpha1-2Galbeta-R, which in this respect resembles mammalian alpha1,2FTs. However, CE2FT-1 is otherwise completely different from known alpha1,2FTs in its acceptor specificity, since it is unable to fucosylate either Galbeta1-4Glcbeta-R or free lactose and prefers the unusual acceptors Galbeta1-4Xylbeta-R and Galbeta1-6GlcNAc-R. Promoter analysis of the CE2FT-1 gene using green fluorescent protein reporter constructs demonstrates that CE2FT-1 is expressed in single cells of early stage embryos and exclusively in the 20 intestinal cells of L(1)-L(4) and adult worms. These and other results suggest that multiple fucosyltransferase genes in C. elegans may encode enzymes with unique activities, expression, and developmental roles.
Authors:
Qinlong Zheng; Irma Van Die; Richard D Cummings
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2002-08-05
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Oct 
Date Detail:
Created Date:  2002-10-15     Completed Date:  2002-12-19     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  39823-32     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Animals, Genetically Modified
Base Sequence
Blotting, Western
Caenorhabditis elegans / enzymology*,  genetics*
Cloning, Molecular
DNA / metabolism
DNA, Complementary / metabolism
Fucosyltransferases / chemistry*,  genetics*
Genes, Reporter
Green Fluorescent Proteins
Humans
Luminescent Proteins / metabolism
Mice
Models, Biological
Molecular Sequence Data
Plasmids / metabolism
Promoter Regions, Genetic
Protein Structure, Tertiary
RNA, Messenger / metabolism
Rabbits
Recombinant Proteins / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Swine
Grant Support
ID/Acronym/Agency:
R01 HD037549/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/Luminescent Proteins; 0/RNA, Messenger; 0/Recombinant Proteins; 147336-22-9/Green Fluorescent Proteins; 9007-49-2/DNA; EC 2.4.1.-/Fucosyltransferases; EC 2.4.1.69/galactoside 2-alpha-L-fucosyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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