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Molecular and Cellular Biology, July 2006, p. 5146-5154, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.02374-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Protein-Protein and Protein-RNA Contacts both Contribute to the 15.5K-Mediated Assembly of the U4/U6 snRNP and the Box C/D snoRNPs

Annemarie Schultz, Stephanie Nottrott,{dagger} Nicholas James Watkins,* and Reinhard Lührmann*

Max Planck Institute of Biophysical Chemistry, Am Faßberg 11, D-37070 Göttingen, Germany

Received 13 December 2005/ Returned for modification 1 February 2006/ Accepted 3 April 2006

The k-turn-binding protein 15.5K is unique in that it is essential for the hierarchical assembly of three RNP complexes distinct in both composition and function, namely, the U4/U6 snRNP, the box C/D snoRNP, and the RNP complex assembled on the U3 box B/C motif. 15.5K interacts with the cognate RNAs via an induced fit mechanism, which results in the folding of the surrounding RNA to create a binding site(s) for the RNP-specific proteins. However, it is possible that 15.5K also mediates RNP formation via protein-protein interactions with the complex-specific proteins. To investigate this possibility, we created a series of 15.5K mutations in which the surface properties of the protein had been changed. We assessed their ability to support the formation of the three distinct RNP complexes and found that the formation of each RNP requires a distinct set of regions on the surface of 15.5K. This implies that protein-protein contacts are essential for RNP formation in each complex. Further supporting this idea, direct protein-protein interaction could be observed between hU3-55K and 15.5K. In conclusion, our data suggest that the formation of each RNP involves the direct recognition of specific elements in both 15.5K protein and the specific RNA.

* Corresponding author. Present address for Nicholas J. Watkins: Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, United Kingdom. Phone: 0044 191 222 6991. Fax: 0044 191 222 7424. E-mail: n.j.watkins{at}ncl.ac.uk. Mailing address for Reinhard Lührmann: Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, Am Faßberg 11, D-3070 Göttingen, Germany.

{dagger} Present address: Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605.

Molecular and Cellular Biology, July 2006, p. 5146-5154, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.02374-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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