Molecular characterization of SUMO E2 conjugation enzyme : differential expression profile in Schistosoma mansoni.
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2011
Autores
Pereira, Roberta Verciano
Cabral, Fernanda Janku
Gomes, Matheus de Souza
Babá, Élio Hideo
Passos, Liana Konovaloff Jannotti
Carvalho, Omar
Rodrigues, Vanderlei
Afonso, Robson José de Cássia Franco
Borges, William de Castro
Cota, Renata Guerra de Sá
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SUMO-dependent post-translational modification
is implicated in a variety of cellular functions including
gene expression regulation, nuclear sub-localization, and
signal transduction. Conjugation of SUMO to other
proteins occurs in a similar process to ubiquitination, which
involves three classes of enzymes: an E1 activating, an E2
conjugating, and an E3 target-specific ligase. Ubc9 is the
unique SUMO E2 enzyme known to conjugate SUMO to
target substrates. Here, we present the molecular characterization
of this enzyme and demonstrate its expression profile
during the S. mansoni life cycle. We have used bioinformatic
approaches to identify the SUMO-conjugating enzyme, the
SmUbc9-like protein, in the Schistosoma mansoni databases.
Quantitative RT-PCR was employed to measure the transcript
levels of SUMO E2 in cercariae, adult worms, and in vitro
cultivated schistosomula. Furthermore, recombinant SmUbc9
was expressed using the Gateway system, and antibodies
raised in rats were used to measure SmUbc9 protein levels in
S. mansoni stages by Western blotting. Our data revealed
upregulation of the SmUbc9 transcript in early schistosomula
followed by a marked differential gene expression in the other
analyzed stages. The protein levels were maintained fairly
constant suggesting a post-transcriptional regulation of
the SmUbc9 mRNA. Our results show for the first time
that S. mansoni employs a functional SUMO E2 enzyme,
for the conjugation of the SUMO proteins to its target
substrates.
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PEREIRA, R. V. et al. Molecular characterization of SUMO E2 conjugation enzyme : differential expression profile in Schistosoma mansoni. Parasitology Research, v. 108, p. 1537-1546, 2011. Disponível em: <https://link.springer.com/article/10.1007%2Fs00436-011-2394-4>. Acesso em: 23 fev. 2017.