TY - JOUR
T1 - Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins
AU - Ismaïli, Naïma
AU - Pérez-Morga, David
AU - Walsh, Patrick
AU - Mayeda, Akila
AU - Pays, Annette
AU - Tebabi, Patricia
AU - Krainer, Adrian R.
AU - Pays, Etienne
N1 - Funding Information:
We acknowledge D. Nolan and M. Berberof for helpful comments and R. Brent, J. Wu, and H. Eisen for providing us with either material or support, or both. This work was supported by research contracts with the Communauté Française de Belgique (ARC), by the Belgian Fonds de la Recherche Scientifique (FRSM and Crédit aux Chercheurs) and by the Interuniversity Poles of Attraction Programme-Belgian State, Prime Minister’s Office-Federal Office for Scientific, Technical and Cultural Affairs. N.I. thanks the Brachet Foundation for help. D.P.M. was an EMBO fellowship recipient during the development of this work.
PY - 1999/7/30
Y1 - 1999/7/30
N2 - The protozoan parasite Trypanosoma brucei relies on trans-splicing to process its mRNAs. A novel nuclear serine/arginine (SR)-rich trypanosomal protein (TSR1) was characterized which contains two RNA recognition motifs. The TSR1 protein appears to be homologous to RNA-binding SR proteins of the cis-splicing machinery from higher eukaryotes. Moreover, in the yeast two-hybrid system, TSR1 is able to interact with the human splicing factors involved in the recognition of the 3' splicing site (U2AF35/U2AF65). In both procyclic and bloodstream forms of T. brucei, TSR1 was found to localize in the nucleus. In the bloodstream stage TSR1 showed the speckles pattern characteristic of SR proteins involved in cis-splicing. Moreover, TSR1 was able to specifically bind the spliced leader (SL) RNA involved in trans-splicing in trypanosomes by the yeast three-hybrid system. These and other observations suggest that TSR1 may be involved in trans-splicing in T. brucei. Copyright (C) 1999 Elsevier Science B.V.
AB - The protozoan parasite Trypanosoma brucei relies on trans-splicing to process its mRNAs. A novel nuclear serine/arginine (SR)-rich trypanosomal protein (TSR1) was characterized which contains two RNA recognition motifs. The TSR1 protein appears to be homologous to RNA-binding SR proteins of the cis-splicing machinery from higher eukaryotes. Moreover, in the yeast two-hybrid system, TSR1 is able to interact with the human splicing factors involved in the recognition of the 3' splicing site (U2AF35/U2AF65). In both procyclic and bloodstream forms of T. brucei, TSR1 was found to localize in the nucleus. In the bloodstream stage TSR1 showed the speckles pattern characteristic of SR proteins involved in cis-splicing. Moreover, TSR1 was able to specifically bind the spliced leader (SL) RNA involved in trans-splicing in trypanosomes by the yeast three-hybrid system. These and other observations suggest that TSR1 may be involved in trans-splicing in T. brucei. Copyright (C) 1999 Elsevier Science B.V.
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U2 - 10.1016/S0166-6851(99)00091-2
DO - 10.1016/S0166-6851(99)00091-2
M3 - Article
C2 - 10477180
AN - SCOPUS:0032800842
VL - 102
SP - 103
EP - 115
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
SN - 0166-6851
IS - 1
ER -