Ubiquitin-conjugating enzyme genes in Oesophagostomum dentatum.
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.
Cottee
Pauline A
PA
Department of Veterinary Science, The University of Melbourne, 250 Princes Highway, Werribee, Victoria 3030, Australia.
Abs EL-Osta
Youssef G
YG
Nisbet
Alasdair J
AJ
Gasser
Robin B
RB
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D019295:Computational Biology / Q000379:methods; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007527:Isoenzymes; D051379:Mice; D008969:Molecular Sequence Data; D009815:Oesophagostomum / Q000201:enzymology* / Q000235:genetics* / Q000254:growth & development; D017422:Sequence Analysis, DNA; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D015801:Helminth Proteins; D007527:Isoenzymes; D044763:Ubiquitin-Conjugating Enzymes