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. 1995 May 9;92(10):4422–4426. doi: 10.1073/pnas.92.10.4422

Catalytically critical nucleotide in domain 5 of a group II intron.

C L Peebles 1, M Zhang 1, P S Perlman 1, J S Franzen 1
PMCID: PMC41956  PMID: 7538669

Abstract

Domain 5 (D5) is a small hairpin structure within group II introns. A bimolecular assay system depends on binding by D5 to an intron substrate for self-splicing activity. In this study, mutations in D5 identify two among six nearly invariant nucleotides as being critical for 5' splice junction hydrolysis but unimportant for binding. A mutation at another site in D5 blocks binding. Thus, mutations can distinguish two D5 functions: substrate binding and catalysis. The secondary structure of D5 may resemble helix I formed by the U2 and U6 small nuclear RNAs in the eukaryotic spliceosome. Our results support a revision of the previously proposed correspondence between D5 and helix I on the basis of the critical trinucleotide 5'-AGC-3' present in both. We suggest that this trinucleotide plays a similar role in promoting the chemical reactions for both splicing systems.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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