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Markus Bohnsack publishes new paper in Molecular Cell

November 2009

RNA helicases play key roles in multiple cellular pathways, such as splicing, translation and RNP transport, while their biological substrates have mostly remained unknown. Several such proteins are required for the biogenesis of ribosomes, which in turn mediate the production of all cellular proteins.  In collaboration with the laboratory of David Tollervey at the University of Edinburgh (UK) the Frankfurt scientists have analysed the molecular functions of the RNA helicase Prp43 in the assembly of eukaryotic ribosomes. Using novel techniques to study RNA-protein interactions the authors identify binding sites of Prp43 on pre-ribosomal RNA and show that the RNA helicase performs several distinct functions in the ribosome biogenesis pathway. At different sites, Prp43 allows release of a cluster of small nucleolar RNAs (snoRNAs), facilitates pre-rRNA binding of other snoRNAs, and promotes pre-rRNA cleavage.

The new paper in Molecular Cell is the first report that identifies binding sites of a eukaryotic RNA helicase on pre-ribosomal RNA. The methods used by Markus Bohnsack and colleagues can be applied for other in vivo studies of transient RNA-protein interactions in multiple cellular pathways.

Full reference: Bohnsack, M.T., Martin, R., Granneman, S., Ruprecht, M., Schleiff, E., Tollervey, D. (2009) Prp43 Bound at Different Sites on the Pre-rRNA Performs Distinct Functions in Ribosome Synthesis. Mol. Cell 36, 583-592.


Full paper

Please contact Markus T. Bohnsack (bohnsack@bio.uni-frankfurt.de) for further information.