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J Biol Chem, Vol. 273, Issue 34, 21825-21833, August 21, 1998
From the Department of Molecular Biology, Free University of
Brussels, 67 rue des Chevaux, B1640 Rhode St. Genèse, Belgium,
§ Department of Biochemistry, Academic Medical Centre,
University of Amsterdam, Meibergdreef 15, 1105 AZ, Amsterdam, The
Netherlands, and ¶ Gene Centre Munich, Max-Planck Institute for
Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
We report the characterization of a
Trypanosoma brucei 75-kDa protein of the RGG (Arg-Gly-Gly)
type, termed TBRGG1. Dicistronic and monocistronic transcripts of the
TBRGG1 gene were produced by both alternative splicing and
polyadenylation. TBRGG1 was found in two or three forms that differ in
their electrophoretic mobility on SDS-polyacrylamide gel
electrophoresis gels, one of which was more abundant in the procyclic
form of the parasite. TBRGG1 was localized to the mitochondrion and
appeared to be more abundant in bloodstream intermediate and stumpy
forms in which the mitochondrion reactivates and during the procyclic
stage, which possesses a fully functional mitochondrion. This protein
was characterized to display oligo(U) binding characteristics and was
found to co-localize with an in vitro RNA editing activity
in a sedimentation analysis. TBRGG1 most likely corresponds to the
83-kDa oligo(U)-binding protein previously identified by UV
cross-linking of guide RNA to mitochondrial lysates (Leegwater, P.,
Speijer, D., and Benne, R. (1995) Eur. J. Biochem.
227, 780-786).
Trypanosoma brucei TBRGG1, a Mitochondrial
Oligo(U)-binding Protein That Co-localizes with an in Vitro
RNA Editing Activity
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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