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Nucleic Acids Research, 1989, Vol. 17, No. 11 4205-4216
© 1989

MOLECULAR BIOLOGY

Structure-function relationships in a self-splicing group II intron: a large part of domain II of the mitochondrial intron al5 is not essential for self-splicing

Jan H.J.M. Kwakman, Danielle Konings1, Herman J. Pel and Leslie A. Grivell

1Section for Biocomputing EMBL, Meyerhofstrasse 1, D6900 Heidelberg, FRG Section for Molecular Biology, Department of Molecular Cell Biology, University of Amsterdam Kruislaan 318, 1098 SM Amsterdam, The Netherlands

Received March 30, 1989. Accepted April 28, 1989.

An oligonucleotide-directed deletion of 156 nucleotides has been introduced into the yeast mitochondrial group II intron al5 (887 nt). The deletion comprises almost all of domain II, which is one of the six phylogenetically conserved structural elements of group II introns. This mutant displays reduced self-splicing activity, but results of chemical probing with dimethylsulphate suggest that sequences at the site of the deletion interfere with the normal folding of the intron. This is supported by computer analyses, which predict a number of alternative structures involving conserved intron sequences.

Splicing activity could be restored by insertion of a 10-nucleotide palindromic sequence into the unique Smal site of the deletion mutant, resulting in the formation of a small stable stem-loop element at the position of domain II. These results provide a direct correlation between folding of the RNA and its activity. We conclude that at least a large part of domain II of the group II intron al5 is not required for self-splicing activity. This deletion mutant with a length of 731 nucleotides represents the smallest self-splicing group II intron so far known.


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