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EMBO reports 8, 4, 408–413 (2007)
doi:10.1038/sj.embor.7400930
AOP Published online: 9 March 2007
Spliced-leader RNA silencing: a novel stress-induced mechanism in Trypanosoma brucei
Yaniv Lustig1, Lilach Sheiner1, Yaron Vagima1, Hanoch Goldshmidt1, Anish Das2, Vivian Bellofatto2 & Shulamit Michaeli1
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1 The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel
2 Department of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, Newark, NJ, USA
To whom correspondence should be addressed
Shulamit Michaeli Tel: +972 3 5318068; Fax: +972 3 7384058; E-mail: michaes@mail.biu.ac.il
Received 20 June 2006; Accepted 23 January 2007; Published online 9 March 2007.
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Abstract
The signal-recognition particle (SRP) mediates the translocation of membrane and secretory proteins across the endoplasmic reticulum upon interaction with the SRP receptor. In trypanosomes, the main RNA molecule is the spliced-leader (SL) RNA, which donates the SL sequence to all messenger RNA through trans-splicing. Here, we show that RNA interference silencing of the SRP receptor (SR ) in Trypanosoma brucei caused the accumulation of SRP on ribosomes and triggered silencing of SL RNA (SLS). SLS was elicited due to the failure of the SL RNA-specific transcription factor tSNAP42 to bind to its promoter. SL RNA reduction, in turn, eliminated mRNA processing and resulted in a significant reduction of all mRNA tested. SLS was also induced under pH stress and might function as a master regulator in trypanosomes. SLS is reminiscent of, but distinct from, the unfolded protein response and can potentially act as a new target for parasite eradication.
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