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Preliminary study of the enzyme ubiquitin carboxylterminal hydrolase 14 (UBP6) in Giardia intestinalis: structural bioinformatic analysis and transcriptional profile during encystation
DOI:
https://doi.org/10.15446/rev.colomb.quim.v43n2.53122Palabras clave:
deubiquitinating enzymes, ubiquitin, Giardia intestinalis, encystation (es)
with two aims. The first is to analyze the
reported sequence of the enzyme ubiquitin
carboxyl-terminal hydrolase 14 of Giardia
intestinalis (UBP6) through computational
methods to find components related with
its hypothetical function. The second is
to determine if the protein-coding gene is
expressed in G. intestinalis and, if such is
the case, also determine its transcription
pattern along the life cycle of the parasite. It
was established that the protein belongs to
the family of Cys-dependent deubiquitinases
and more specifically to ubiquitin specific
proteases (USPs). Moreover, the catalytic
center with the complete triad as well as
typical features of the USP motif were also
identified. Since the computational findings
suggest that the enzyme could be functional,
reverse transcription coupled to PCR was
used as a first approach to establish if in fact
the coding gene is expressed in the parasite.
Interestingly, it was found not only that
the gene is expressed, but also that there
is a transcription variation along the life
cycle of the parasite. These two findings are
the starting point for further studies since
they tentatively suggest that this enzyme
could be involved in the protein turnover
that occurs during parasite encystation.
Although preliminary, this study is the first
report concerning the study of a specific
deubiquitinating enzyme in the parasite G.
intestinalis.
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