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- W41870321 abstract "Splicing is an essential step in the maturation of eukaryotic pre-mRNA in which intervening sequences (introns) are removed from the coding sequences (exons). The spliceosome is a dynamic assembly of five snRNAs and over 150 proteins that catalyzes splicing. U2 and U6 are two snRNAs that form an RNA complex strictly required for both steps of splicing. Major conformational changes are expected to take place during the assembly and catalysis of the spliceosome. We have used Fluorescence Resonance Energy Transfer (FRET) and Single Molecule Spectroscopy to study the structural dynamics of a protein free U2-U6 complex from yeast. Our bulk data clearly shows a Mg2+ induced large amplitude conformation change of the U2-U6 complex. In the absence of Mg2+, helix I and the U6-ISL are in close proximity, while in the presence of Mg2+ these two helices are far from each other. Our single molecule data reveals that this conformational change consists of a two-step process with an obligatory folding intermediate. We propose that the observed conformational change corresponds to the activation process expected to occur during spliceosomal assembly and catalysis. We are currently investigating this hypothesis by introducing mutations in highly conserved regions of the U2-U6 complex." @default.
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- W41870321 date "2007-01-01" @default.
- W41870321 modified "2023-10-17" @default.
- W41870321 title "Structural Dynamics of Single Spliceosomal RNAs U2/U6" @default.
- W41870321 doi "https://doi.org/10.1096/fasebj.21.6.lb30-c" @default.
- W41870321 hasPublicationYear "2007" @default.
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