Document Detail


Molecular cloning of a developmentally regulated N-acetylgalactosamine alpha2,6-sialyltransferase specific for sialylated glycoconjugates.
MedLine Citation:
PMID:  8631773     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A cDNA encoding a novel sialyltransferase has been isolated employing the polymerase chain reaction using degenerate primers to conserved regions of the sialylmotif that is present in all eukaryotic members of the sialyltransferase gene family examined to date. The cDNA sequence revealed an open reading frame coding for 305 amino acids, making it the shortest sialyltransferase cloned to date. This open reading frame predicts all the characteristic structural features of other sialyltransferases including a type II membrane protein topology and both sialylmotifs, one centrally located and the second in the carboxyl-terminal portion of the cDNA. When compared with all other sialyltransferase cDNAs, the predicted amino acid sequence displays the lowest homology in the sialyltransferase gene family. Northern analysis shows this sialyltransferase to be developmentally regulated in brain with expression persisting through adulthood in spleen, kidney, and lung. Stable transfection of the full-length cDNA in the human kidney carcinoma cell line 293 produced an active sialyltransferase with marked specificity for the sialoside, Neu5Ac-alpha2,3Gal-beta1,3GalNAc and glycoconjugates carrying the same sequence such as G(M1b) and fetuin. The disialylated tetrasaccharide formed by reacting the sialyltransferase with the aforementioned sialoside was analyzed by one- and two-dimensional 1H and 13C NMR spectroscopy and was shown to be the Neu5Ac-alpha2,3Gal-beta1,3(Neu5Ac-alpha2,6)GalNAc sialoside. This indicates that the enzyme is a GalNAc alpha-2,6-sialyltransferase. Since two other ST6GalNAc sialyltransferase cDNAs have been isolated, this sialyltransferase has been designated ST6GalNAc III. Of these three, ST6GalNAc III displays the most restricted acceptor specificity and is the only sialyltransferase cloned to date capable of forming the developmentally regulated ganglioside G(D1alpha) from G(M1b).
Authors:
E R Sjoberg; H Kitagawa; J Glushka; H van Halbeek; J C Paulson
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  271     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1996 Mar 
Date Detail:
Created Date:  1996-07-03     Completed Date:  1996-07-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7450-9     Citation Subset:  IM    
Affiliation:
Cytel Corporation, San Diego, California, 92121, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/L29554
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Carbohydrate Sequence
Chickens
Cloning, Molecular
Consensus Sequence
Conserved Sequence
DNA Primers
DNA, Complementary
Gene Expression Regulation, Enzymologic*
Glycoconjugates / metabolism*
Humans
Magnetic Resonance Spectroscopy
Membrane Proteins / biosynthesis,  metabolism
Mice
Molecular Sequence Data
Multigene Family*
Oligosaccharides / chemical synthesis,  metabolism
Open Reading Frames
Polymerase Chain Reaction
Rats
Recombinant Proteins / biosynthesis,  metabolism
Sequence Homology, Amino Acid
Sialic Acids
Sialyltransferases / biosynthesis,  chemistry,  metabolism*
Substrate Specificity
Grant Support
ID/Acronym/Agency:
GM 27904/GM/NIGMS NIH HHS; P41-RR-05351/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/DNA Primers; 0/DNA, Complementary; 0/Glycoconjugates; 0/Membrane Proteins; 0/Oligosaccharides; 0/Recombinant Proteins; 0/Sialic Acids; EC 2.4.99.-/Neu5Ac N-acetylgalactosamine 2,6-sialyltransferase; EC 2.4.99.-/Sialyltransferases

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