Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins

Naïma Ismaïli; David Pérez-Morga; Patrick Walsh; Akila Mayeda; Annette Pays; Patricia Tebabi; Adrian R. Krainer; Etienne Pays

doi:10.1016/S0166-6851(99)00091-2

Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins

Naïma Ismaïli, David Pérez-Morga, Patrick Walsh, Akila Mayeda, Annette Pays, Patricia Tebabi, Adrian R. Krainer, Etienne Pays

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

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	https://doi.org/10.1016/S0166-6851(99)00091-2
Publication status	Published - 30-07-1999
Externally published	Yes

All Science Journal Classification (ASJC) codes

Parasitology
Molecular Biology

Access to Document

10.1016/S0166-6851(99)00091-2

Cite this

@article{dfaaf50c8e554ebc9bba0b7956d97c02,

title = "Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins",

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.",

keywords = "RRM motif, SR protein, Spliced leader RNA, Trypanosoma brucei, trans-splicing",

author = "Na{\"i}ma Isma{\"i}li and David P{\'e}rez-Morga and Patrick Walsh and Akila Mayeda and Annette Pays and Patricia Tebabi and Krainer, {Adrian R.} and Etienne Pays",

note = "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 Communaut{\'e} Fran{\c c}aise de Belgique (ARC), by the Belgian Fonds de la Recherche Scientifique (FRSM and Cr{\'e}dit aux Chercheurs) and by the Interuniversity Poles of Attraction Programme-Belgian State, Prime Minister{\textquoteright}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.",

year = "1999",

month = jul,

day = "30",

doi = "10.1016/S0166-6851(99)00091-2",

language = "English",

volume = "102",

pages = "103--115",

journal = "Molecular and Biochemical Parasitology",

issn = "0166-6851",

publisher = "Elsevier B.V.",

number = "1",

}

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.

KW - RRM motif

KW - SR protein

KW - Spliced leader RNA

KW - Trypanosoma brucei

KW - trans-splicing

UR - http://www.scopus.com/inward/record.url?scp=0032800842&partnerID=8YFLogxK

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

C2 - 10477180

AN - SCOPUS:0032800842

SN - 0166-6851

VL - 102

SP - 103

EP - 115

JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

IS - 1

ER -

Characterization of a SR protein from Trypanosoma brucei with homology to RNA-binding cis-splicing proteins

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this