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Originally published In Press as doi:10.1074/jbc.M209215200 on February 26, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18271-18280, May 16, 2003
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The Trypanosomatid Signal Recognition Particle Consists of Two RNA Molecules, a 7SL RNA Homologue and a Novel tRNA-like Molecule*

Li LiuDagger §, Herzel Ben-Shlomo§||, Yu-xin Xu||, Michael Zeev SternDagger , Igor Goncharov||, Yafei Zhang**, and Shulamit MichaeliDagger Dagger Dagger

From the Dagger  Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900 and the  Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel

Trypanosomatids are ancient eukaryotic parasites affecting humans and livestock. Here we report that the trypanosomatid signal recognition particle (SRP), unlike all other known SRPs in nature, contains, in addition to the 7SL RNA homologue, a short RNA molecule, termed sRNA-85. Using conventional chromatography, we discovered a small RNA molecule of 85 nucleotides co-migrating with the Leptomonas collosoma 7SL RNA. This RNA molecule was isolated, sequenced, and used to clone the corresponding gene. sRNA-85 was identified as a tRNA-like molecule that deviates from the canonical tRNA structure. The co-existence of these RNAs in a single complex was confirmed by affinity selection using an antisense oligonucleotide to sRNA-85. The two RNA molecules exist in a particle of ~14 S that binds transiently to ribosomes. Mutations were introduced in sRNA-85 that disrupted its putative potential to interact with 7SL RNA by base pairing; such mutants were unable to bind to 7SL RNA and to ribosomes and were aberrantly distributed within the cell. We postulate that sRNA-85 may functionally replace the truncated Alu domain of 7SL RNA. The discovery of sRNA-85 raises the intriguing possibility that sRNA-85 functional homologues may exist in other lower eukaryotes and eubacteria that lack the Alu domain.


* This work was supported in part by a research grant from the Israel Academy of Sciences.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY145448.

§ Both authors contributed equally to this work.

|| Graduate students at the Feinberg Graduate School of the Weizmann Institute of Science.

** A visiting student at the Feinberg Graduate School of the Weizmann Institute of Science.

Dagger Dagger A Howard Hughes Institute International Scholar in Molecular Parasitology. To whom correspondence should be addressed. Tel.: 972-3-531-8068; Fax: 972-3-535-1824; E-mail: michaes@mail.biu.ac.il.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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