The excision of introns from eukaryotic pre-mRNA and splicing together of exons is performed by a macromolecular machine called the spliceosome. Splicing is a highly dynamic process that involves many spliceosomal intermediates. Each intermediate contains specific RNA-protein complexes called small nuclear ribonucleoprotein particles (snRNPs) and a number of additional non-snRNP proteins. It has been established that the spliceosome intermediates that are involved in the actual splicing reactions contain U2 , U5 and U6 snRNPs and that their snRNA plays a very important role in catalysing the reactions. To date, the crystal structures of a number of components of snRNPs have been reported. Detailed insight into the mechanism of splicing at the molecular level is, however, hampered by lack of structural information of the larger complexes present at the catalytic site of the spliceosome. Therefore I propose to work on those protein-RNA complexes and subsets of intermediates of the spliceosome that are involved i n the catalytic steps during splicing in crystallographic and biochemical studies.
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