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Nucleic Acids Research 2005 33(8):2493-2503; doi:10.1093/nar/gki548
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Published online 29 April 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

U1 small nuclear RNP from Trypanosoma brucei: a minimal U1 snRNA with unusual protein components

Zsofia Palfi, Bernd Schimanski1,2, Arthur Günzl1,2, Stephan Lücke and Albrecht Bindereif*

Institut für Biochemie, Justus-Liebig-Universität Giessen Heinrich-Buff-Ring 58, D-35392 Giessen, Germany 1Department of Genetics and Developmental Biology, University of Connecticut Health Center Farmington, CT, USA 2Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center Farmington, CT, USA

*To whom correspondence should be addressed. Tel: +49 641 99 35 420; Fax: +49 641 99 35 419; Email: albrecht.bindereif{at}chemie.bio.uni-giessen.de

Received March 15, 2005. Revised April 14, 2005. Accepted April 14, 2005.

Processing of primary transcripts in trypanosomes requires trans splicing and polyadenylation, and at least for the poly(A) polymerase gene, also internal cis splicing. The trypanosome U1 snRNA, which is most likely a cis-splicing specific component, is unusually short and has a relatively simple secondary structure. Here, we report the identification of three specific protein components of the Trypanosoma brucei U1 snRNP, based on mass spectrometry and confirmed by in vivo epitope tagging and in vitro RNA binding. Both T.brucei U1-70K and U1C are only distantly related to known counterparts from other eukaryotes. The T.brucei U1-70K protein represents a minimal version of 70K, recognizing the first loop sequence of U1 snRNA with the same specificity as the mammalian protein. The trypanosome U1C-like protein interacts with 70K directly and binds the 5' terminal sequence of U1 snRNA. Surprisingly, instead of U1A we have identified a novel U1 snRNP-specific protein, TbU1-24K. U1-24K lacks a known RNA-binding motif and integrates in the U1 snRNP via interaction with U1-70K. These data result in a model of the trypanosome U1 snRNP, which deviates substantially from our classical view of the U1 particle and may reflect the special requirements for splicing of a small set of cis-introns in trypanosomes.

Present address: Stephan Lücke, Howard Hughes Medical Institute, Program in Gene Function and Expression, University of Massachusetts Medical School, LRB-670A, 364 Plantation Street, Worcester, MA 01605, USA


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