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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
The Trypanosomatid Signal Recognition Particle Consists of
Two RNA Molecules, a 7SL RNA Homologue and a Novel tRNA-like
Molecule*
Li
Liu §,
Herzel
Ben-Shlomo§¶ ,
Yu-xin
Xu¶ ,
Michael Zeev
Stern ,
Igor
Goncharov¶ ,
Yafei
Zhang¶**, and
Shulamit
Michaeli 
From the 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.

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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