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Volume 272, Number 6, Issue of February 7, 1997 pp. 3749-3757
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Trypanosoma brucei gBP21
AN ARGININE-RICH MITOCHONDRIAL PROTEIN THAT BINDS TO GUIDE RNA WITH HIGH AFFINITY

(Received for publication, August 29, 1996)

Johannes Köller , Ulrich F. Müller , Beate Schmid , Andreas Missel , Volker Kruft Dagger , Kenneth Stuart § and H. Ulrich Göringer

From the Laboratorium für molekulare Biologie, Genzentrum der LMU München am MPI für Biochemie, 82152 Martinsried, Germany, Dagger  PE Applied Biosystems, Brunnenweg 13, 64331 Weiterstadt, Germany, the § Seattle Biomedical Research Institute, Seattle, Washington 98109, and the  Pathobiology Department, SC38, University of Washington, Seattle, Washington 98195

RNA editing in Trypanosoma brucei is a mitochondrial RNA processing reaction that results in the insertion and deletion of uridylate residues into otherwise untranslatable mRNAs. The process is directed by guide RNAs which function to specify the edited sequence. RNA editing in vitro requires mitochondrial protein extracts and guide RNAs have been identified as part of high molecular weight ribonucleoprotein complexes. Within the complexes, the RNAs are in close contact with several mitochondrial proteins and here we describe the isolation and cloning of a gRNA-interacting polypeptide from Trypanosoma brucei. The protein was named gBP21 for <UNL>g</UNL>uide RNA-<UNL>b</UNL>inding <UNL>p</UNL>rotein of <UNL>21</UNL> kDa. gBP21 shows no homology to proteins in other organisms, it is arginine-rich and binds to gRNA molecules with a dissociation constant in the nanomolar range. The protein does not discriminate for differences in the primary structures of gRNAs and thus likely binds to higher order structural features common to all gRNA molecules. gBP21 binding does not perturb the overall structure of gRNAs but the gRNA/gBP21 ribonucleoprotein complex is more stable than naked guide RNAs. Although the protein is arginine-rich, the free amino acid or an arginine-rich peptide were not able to inhibit the association to the RNAs. In contrast, the gRNA-gBP21 complex formation was sensitive to potassium and ammonium cations, thus indicating a contribution of ionic contacts to the binding.


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