Ubiquitin-conjugating enzyme genes in Oesophagostomum dentatum.
Parasitol Res
; 99(2): 119-25, 2006 Jul.
Article
em En
| MEDLINE
| ID: mdl-16518612
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oesophagostomum
/
Enzimas de Conjugação de Ubiquitina
Limite:
Animals
Idioma:
En
Revista:
Parasitol Res
Assunto da revista:
PARASITOLOGIA
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Austrália