Key result
The 3' half of the spliced leader RNA constitutes the core protein-binding domain of the SL RNP in Trypanosoma brucei, and a set of low-molecular-mass proteins are components of the core SL RNP.
May inform antiparasitic RNA-targeting strategies; leaves open validation as therapeutic targets in trypanosomiasis.
trans splicing in Trypanosoma brucei involves the ligation of the 40-nucleotide spliced leader (SL) to each of the exons of large, polycistronic pre-mRNAs and requires the function of small nuclear ribonucleoproteins (snRNPs). We have identified and characterized snRNP complexes of SL, U2, U4, and U6 RNAs in T. brucei extracts by a combination of glycerol gradient sedimentation, CsCl density centrifugation, and anti-m3G immunoprecipitation. Both the SL RNP and the U4/U6 snRNP contain salt-stable cores; the U2 snRNP, in contrast to other eucaryotic snRNPs, is not stable under stringent ionic conditions. Two distinct complexes of U6 RNA were found, a U6 snRNP and a U4/U6 snRNP. The structure of the SL RNP was analyzed in detail by oligonucleotide-directed RNase H protection and by in vitro reconstitution. Our results indicate that the 3' half of SL RNA constitutes the core protein-binding domain and that protein components of the SL RNP also bind to the U2 and U4 RNAs. Using antisense RNA affinity chromatography, we identified a set of low-molecular-mass proteins (14.8, 14, 12.5, and 10 kDa) as components of the core SL RNP.
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Cross et al. (1991) studied Trypanosoma brucei (basic science). Biochemical analysis of snRNPs was evaluated. The 3' half of the spliced leader RNA constitutes the core protein-binding domain of the SL RNP in Trypanosoma brucei, and a set of low-molecular-mass proteins are components of the core SL RNP.
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