Investigation on the 19S ATPase proteasome subunits (Rpt1 6) conservation and their differential gene expression in Schistosoma mansoni.

Pereira Junior, Olavo dos Santos; Pereira, Roberta Verciano; Silva, Camila Siqueira; Borges, William de Castro; Cota, Renata Guerra de Sá; Cabral, Fernanda Janku; Silva, Sérgio Henrique da; Soares, Cláudia Sossai; Morais, Enyara Rezende; Moreira, Érika Bueno de Carvalho; Magalhães, Lizandra Guidi; Paula, Fabiana Martins de; Rodrigues, Vanderlei

Investigation on the 19S ATPase proteasome subunits (Rpt1 6) conservation and their differential gene expression in Schistosoma mansoni.

Date

2013

Authors

Pereira Junior, Olavo dos Santos

Pereira, Roberta Verciano

Silva, Camila Siqueira

Borges, William de Castro

Cota, Renata Guerra de Sá

Cabral, Fernanda Janku

Silva, Sérgio Henrique da

Soares, Cláudia Sossai

Morais, Enyara Rezende

Moreira, Érika Bueno de Carvalho

Abstract

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.

Citation

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.