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Prog Mol Biol Transl Sci. 2013;120:195-228. doi: 10.1016/B978-0-12-381286-5.00006-8.

The role of snRNAs in spliceosomal catalysis.

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Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.


The spliceosomes, large ribonucleoprotein (RNP) assemblies that remove the intervening sequences from pre-mRNAs, contain a large number of proteins and five small nuclear RNAs (snRNAs). One snRNA, U6, contains highly conserved sequences that are thought to be the functional counterparts of the RNA elements that form the active site of self-splicing group II intron ribozymes. An in vitro-assembled, protein-free complex of U6 with U2, the base-pairing partner in the spliceosomal catalytic core, can catalyze a two-step splicing reaction in the absence of all other spliceosomal factors, suggesting that the two snRNAs may form all or a large share of the spliceosomal active site. On the other hand, several spliceosomal proteins are thought to help in the formation of functionally required RNA-RNA interactions in the catalytic core. Whether they also contribute functional groups to the spliceosomal active site, and thus whether the spliceosomes are RNA or RNP enzymes remain uncertain.


Catalysis; Group II introns; Prp8; RNA world; Ribozyme; Spliceosome; Splicing; U2; U6; snRNAs

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