Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 103-115 |
| Number of pages | 13 |
| Journal | Molecular and Biochemical Parasitology |
| Volume | 102 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 30-07-1999 |
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All Science Journal Classification (ASJC) codes
- Parasitology
- Molecular Biology
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Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins. / Ismaïli, Naïma; Pérez-Morga, David; Walsh, Patrick; Maeda, Akira; Pays, Annette; Tebabi, Patricia; Krainer, Adrian R.; Pays, Etienne.
In: Molecular and Biochemical Parasitology, Vol. 102, No. 1, 30.07.1999, p. 103-115.Research output: Contribution to journal › Article
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 - Maeda, Akira
AU - Pays, Annette
AU - Tebabi, Patricia
AU - Krainer, Adrian R.
AU - Pays, Etienne
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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UR - http://www.scopus.com/inward/citedby.url?scp=0032800842&partnerID=8YFLogxK
U2 - 10.1016/S0166-6851(99)00091-2
DO - 10.1016/S0166-6851(99)00091-2
M3 - Article
VL - 102
SP - 103
EP - 115
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
SN - 0166-6851
IS - 1
ER -