Böhm, Cordula ; Katari, Venkata Subbaraju ; Brecht, Michael ; Göringer, H. Ulrich (2012)
Trypanosoma brucei 20S editosomes have one RNA substrate-binding site and execute RNA unwinding activity.
In: The Journal of biological chemistry, 287 (31)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Editing of mitochondrial pre-mRNAs in African trypanosomes generates full-length transcripts by the site-specific insertion and deletion of U nucleotides. The reaction is catalyzed by a 0.8MDa multienzyme complex, the editosome. Although the binding of substrate pre-edited mRNAs and cognate gRNAs represents the first step in the reaction cycle, the biochemical and biophysical details of the editosome/RNA interaction are not understood. Here we show that editosomes bind full-length substrate mRNAs with nanomolar affinity in a nonselective fashion. The complexes do not discriminate - neither kinetically nor thermodynamically - between different mitochondrial pre-mRNAs or between edited and unedited versions of the same transcript. They also bind gRNAs and gRNA/pre-mRNA hybrid RNAs with similar affinities and association rate constants. Gold-labeling of editosome-bound RNA in combination with transmission electron microscopy (TEM) identified a single RNA binding site per editosome. However, atomic force microscopy (AFM) of individual pre-mRNA/editosome complexes revealed that multiple editosomes can interact with one pre-mRNA. Lastly, we demonstrate a so far unknown activity of the editing machinery: editosome-bound RNA becomes unfolded by a chaperone-type RNA unwinding activity.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2012 |
| Autor(en): | Böhm, Cordula ; Katari, Venkata Subbaraju ; Brecht, Michael ; Göringer, H. Ulrich |
| Art des Eintrags: | Bibliographie |
| Titel: | Trypanosoma brucei 20S editosomes have one RNA substrate-binding site and execute RNA unwinding activity. |
| Sprache: | Englisch |
| Publikationsjahr: | 2012 |
| Verlag: | American Society for Biochemistry and Molecular Biology |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | The Journal of biological chemistry |
| Jahrgang/Volume einer Zeitschrift: | 287 |
| (Heft-)Nummer: | 31 |
| Kurzbeschreibung (Abstract): | Editing of mitochondrial pre-mRNAs in African trypanosomes generates full-length transcripts by the site-specific insertion and deletion of U nucleotides. The reaction is catalyzed by a 0.8MDa multienzyme complex, the editosome. Although the binding of substrate pre-edited mRNAs and cognate gRNAs represents the first step in the reaction cycle, the biochemical and biophysical details of the editosome/RNA interaction are not understood. Here we show that editosomes bind full-length substrate mRNAs with nanomolar affinity in a nonselective fashion. The complexes do not discriminate - neither kinetically nor thermodynamically - between different mitochondrial pre-mRNAs or between edited and unedited versions of the same transcript. They also bind gRNAs and gRNA/pre-mRNA hybrid RNAs with similar affinities and association rate constants. Gold-labeling of editosome-bound RNA in combination with transmission electron microscopy (TEM) identified a single RNA binding site per editosome. However, atomic force microscopy (AFM) of individual pre-mRNA/editosome complexes revealed that multiple editosomes can interact with one pre-mRNA. Lastly, we demonstrate a so far unknown activity of the editing machinery: editosome-bound RNA becomes unfolded by a chaperone-type RNA unwinding activity. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie > Genregulation und RNA-Therapeutika |
| Hinterlegungsdatum: | 11 Jun 2012 12:32 |
| Letzte Änderung: | 17 Jul 2018 14:22 |
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