Ubiquitin-conjugating enzyme genes in Oesophagostomum dentatum
Ubiquitin-conjugating enzyme genes in Oesophagostomum dentatum
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DOI:
10.1007/s00436-005-0111-x
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发表时间:
2006-07-01
影响因子:
2
通讯作者:
Gasser, Robin B.
中科院分区:
文献类型:
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作者:
Cottee, Pauline A.;El-Osta, Youssef G. Abs;Gasser, Robin B.
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.