Investigation on the 19S ATPase proteasome subunits (Rpt1 6) conservation and their differential gene expression in Schistosoma mansoni.
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2013
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The ubiquitin-proteasome system is responsible
for degradation of the majority of intracellular proteins in
eukaryotic cells. The 26S proteasome proteolytic complex is
composed of a 20S core particle responsible for protein degradation
and the 19S lid which plays a role in the recognition
of polyubiquitinated substrates. The 19S regulatory particle
(Rps) is composed of ATPase (Rpt) and non-ATPase (Rpn)
subunits. In this study, we analyzed the expression profile of
19S Rpt subunits in the larvae and adult stage of the
Schistosoma mansoni life cycle. Conventional reverse transcriptase
polymerase chain reaction (RT-PCR) revealed that
the majority of the 19S Rpt subunits amplified at the expected
molecular masses for various investigated stages. In addition,
SmRpt1, SmRpt2, and SmRpt6 transcript levels were increased
in 3 h-cultured schistosomula and reasonably maintained
until 5 h in culture, as revealed by qRT-PCR.
Phylogenetic analysis of 19S Rpt subunits showed high structural
conservation in comparison to other Rpt orthologues.
The mRNA expression profile of 19S Rpt subunits did not
correlate with 26S proteasome proteolytic activity as judged
by a 14C-casein-degrading assay, in the early cultured schistosomula.
Taken together, these results revealed a differential
expression profile for 19S Rpt subunits whose transcript levels
could not be directly associated to 26S proteasome activity.
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PEREIRA JÚNIOR, O. dos S. et al. Investigation on the 19S ATPase proteasome subunits (Rpt1 6) conservation and their differential gene expression in Schistosoma mansoni. Parasitology Research, v. 112, p. 235-242, 2012. Disponível em: <https://link.springer.com/article/10.1007%2Fs00436-012-3130-4>. Acesso em: 23 fev. 2017.