Ubiquitin-conjugating Enzyme Genes in Oesophagostomum Dentatum.
From: Department of Veterinary Science, The University of Melbourne, 250 Princes Highway, Werribee, Victoria 3030, Australia.
Parasitology research
- Publish Date: Jul 2006
- ISSN: 0932-0113
- Volume: 99
- Issue: 2
- Pages: 119-25
- Medium: Print
- Language: English
- Citation (JAMA): Cottee Pauline A, Abs EL-Osta Youssef G, Nisbet Alasdair J, et al. Ubiquitin-conjugating Enzyme Genes in Oesophagostomum Dentatum.. Parasitol. Res. Jul 2006;99:119-25
Abstract
Full-length genes representing different isoforms of the ubiquitin-conjugating enzyme UBC-2 were isolated from Oesophagostomum dentatum, cloned and sequenced. The alignment of their sequences (designated Od-ubc-2.1 to Od-ubc-2.3) revealed nucleotide variation at three positions within the predicted open reading frame of 444 bp. Substitutions were at positions 141 (A< — >G), 142 (A< — >G) and 296 (T< — >C). Both former substitutions resulted in amino acid changes from a glycine residue to an arginine residue, whereas the latter resulted in a change from isoleucine to threonine. Comparison of predicted OD-UBC-2 with UBC-2 (protein) homologues/orthologues from 12 other species representing nematodes, Drosophila melanogaster, Saccharomyces cerevisiae, mice and humans revealed identities between species varying from 77 to 100% at the amino acid level, and motifs associated with protein conformation and function were identified. While the function of a representative ubc-2 gene from O. dentatum could not be established in C. elegans, it is likely to play a key role in the catabolism of proteins and in the development of O. dentatum.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Computational Biology, Helminth Proteins, Isoenzymes, Mice, Molecular Sequence Data, Oesophagostomum, Sequence Analysis, DNA, Ubiquitin-Conjugating Enzymes
Check for Full Text / PubMed Unique Identifier (PMID): 16518612
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