Transcriptional profile and structural conservation of SUMO-Specific proteases in schistosoma mansoni.
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2012
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Abstract
Small ubiquitin-related modifier (SUMO) is involved in numerous cellular processes including protein localization, transcription,
and cell cycle control. SUMOylation is a dynamic process, catalyzed by three SUMO-specific enzymes and reversed by
Sentrin/SUMO-specific proteases (SENPs). Here we report the characterization of these proteases in Schistosoma mansoni. Using
in silico analysis, we identified two SENPs sequences, orthologs of mammalian SENP1 and SENP7, confirming their identities
and conservation through phylogenetic analysis. In addition, the transcript levels of Smsenp1/7 in cercariae, adult worms, and
in vitro cultivated schistosomula were measured by qRT-PCR. Our data revealed upregulation of the Smsenp1/7 transcripts in
cercariae and early schistosomula, followed by a marked differential gene expression in the other analyzed stages. However, no
significant difference in expression profile between the paralogs was observed for the analyzed stages. Furthermore, in order
to detect deSUMOylating capabilities in crude parasite extracts, SmSENP1 enzymatic activity was evaluated using SUMO-1-
AMC substrate. The endopeptidase activity related to SUMO-1 precursor processing did not differ significantly between cercariae
and adult worms. Taken together, these results support the developmentally regulated expression of SUMO-specific proteases in
S. mansoni.
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PEREIRA, R. V. et al. Transcriptional profile and structural conservation of SUMO-Specific proteases in schistosoma mansoni. Journal of Parasitology, v. 2012, p. 1-7, 2012. Disponível em: <https://www.hindawi.com/journals/jpr/2012/480824/>. Acesso em: 23 fev. 2017.