Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Warren, C. E.
Right arrow Articles by Dennis, J. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Warren, C. E.
Right arrow Articles by Dennis, J. W.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2001, Vol. 11, No. 11 979-988
© 2001 Oxford University Press

Complementary expression patterns of six nonessential Caenorhabditis elegans core 2/I N-acetylglucosaminyltransferase homologues

Charles E. Warren2, Aldis Krizus2 and James W. Dennis1,2,3

2Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada, and 3Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, Canada

The Caenorhabditis elegans genome contains 18 sequences related to mammalian core 2/I N-acetylglucosaminyltransferases. The six most closely related genes (gly-1 and gly-15 to gly-19) likely encode active enzymes, because are all transcribed and do not appear to be pseudogenes. Polypeptide divergence and the gene structures are both concordant with a common ancestor at the time of radiation from mammals that underwent three rounds of duplication and, most recently, a tandem duplication. Polypeptide alignments with mammalian homologues do not indicate whether the enzyme specificities are core 2, 4, or I-like or novel, but do clearly demonstrate the secondary structure characteristics of glycosyltransferases. The six homologues have essentially nonoverlapping expression patterns, unrelated by tissue type or cell lineage. The extent varies widely; gly-15 is expressed only in two gland cells, whereas gly-18 is broadly expressed in diverse cell types. gly-1, -15, -18 and -19 are expressed during adulthood; gly-16 and gly-17 appear to be restricted to embryonic or early larval stages. The parsimonious interpretation of the expression pattern and sequence data is that the catalytic activities are similar but with diverged promoters. Null alleles of three of the genes were generated without causing gross abnormality in homozygous animals. RNA-mediated interference experiments also failed to induce defects in the four genes tested. Nevertheless, the nematode has evolved six diverged core 2 GlcNAc-T–like genes, and we postulate that these arose in response to selection pressures to which C. elegans is not ordinarily subjected in the laboratory.

1 To whom correspondence should be addressed


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
K. Nguyen, I. van Die, K. M Grundahl, Z. S Kawar, and R. D Cummings
Molecular cloning and characterization of the Caenorhabditis elegans {alpha}1,3-fucosyltransferase family
Glycobiology, June 1, 2007; 17(6): 586 - 599.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Q. Zheng, I. Van Die, and R. D. Cummings
Molecular Cloning and Characterization of a Novel alpha 1,2-Fucosyltransferase (CE2FT-1) from Caenorhabditis elegans
J. Biol. Chem., October 11, 2002; 277(42): 39823 - 39832.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. E. Warren, A. Krizus, P. J. Roy, J. G. Culotti, and J. W. Dennis
The Caenorhabditis elegans Gene, gly-2, Can Rescue the N-Acetylglucosaminyltransferase V Mutation of Lec4 Cells
J. Biol. Chem., June 14, 2002; 277(25): 22829 - 22838.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. B. H. Wilson
Functional Characterization of Drosophila melanogaster Peptide O-Xylosyltransferase, the Key Enzyme for Proteoglycan Chain Initiation and Member of the Core 2/I N-Acetylglucosaminyltransferase Family
J. Biol. Chem., June 7, 2002; 277(24): 21207 - 21212.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.