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Eukaryotic Cell doi:10.1128/EC.00279-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

SSU rRNA processome proteins are translationally regulated during differentiation of Trypanosoma cruzi

Instituto de Biologia Molecular do Paraná, Rua Professor Algacyr Munhoz Mader 3775, Curitiba 81350-010, PR, Brazil, FIOCRUZ, Avenida Brasil 4365, Rio de Janeiro, 21040-900, RJ, Brazil, Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro 21949-900, RJ, Brazil, Departamento de Microbiologia, Imunologia e Parasitologia, Rua Botucatu 862-8a, UNIFESP, São Paulo 04023-062, SP, Brazil

^* To whom correspondence should be addressed. Email: sgoldenb{at}tecpar.br,

	Abstract

We used differential display to select genes differentially expressed during differentiation of epimastigotes into metacyclic trypomastigotes in the protozoan parasite Trypanosoma cruzi. One of the selected clones had a sequence similar to that of the SSU processome protein Sof1p involved in rRNA processing. The corresponding T. cruzi protein, TcSof1, displayed a nuclear localization and is downregulated during metacyclogenesis. Heterologous RNA interference assays showed that depletion of this protein impaired growth but did not affect progression through the cell cycle, suggesting that ribosome synthesis regulation and the cell cycle are uncoupled in this parasite. Quantitative PCR assays of several SSU processome-specific genes in T. cruzi also showed that most of them were regulated posttranscriptionally. This process involves the accumulation of mRNA in the polysome fraction of metacyclic trypomastigotes where TcSof1 can not be detected. Metacyclic trypomastigote polysomes were purified and separated by sucrose gradient sedimentation. Northern blot analysis of the sucrose gradient fractions showed the association of TcSof1 mRNA with polysomes, confirming the qPCR data. The results suggest that the mechanism of regulation involves the blocking of translation elongation and/or termination.

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