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Nucleic Acids Research, 1992, Vol. 20, No. 17 4473-4479
© 1992

MOLECULAR BIOLOGY

The mechanisms controlling ribosomal protein L1 pre-mRNA splicing are maintained in evolution and rely on conserved intron sequences

Silvia Prislei1, Sabina Sperandio1, Paola Fragapane, Elisa Caffarelli, Carlo Presutti1 and Irene Bozzoni1,*

Centro Acidi Nucleici, CNR Rome 1Istituto Pasteur Fondazione Cenci Bolognetti, Dipartimento di Genetica e Biologia Molecolare, Università ‘La Sapienza’ Rome, Italy

*To whom correspondence should be addressed

Received June 11, 1992. Revised July 31, 1992. Accepted July 31, 1992.

Sequences corresponding to the third intron of the X.laevis L1 ribosomal protein gene were isolated from the second copy of the X.laevis gene and from the single copy of X.tropicalls. Sequence comparison revealed that the three Introns share an unusual sequence conservation which spans a region of 110 nucleotides. In addition, they have the same suboptimal 5' splice sites. The three introns show similar features upon oocyte microinjection: they have very low splicing efficiency and undergo the same site specific cleavages which lead to the accumulation of truncated molecules. Computer analysis and RNAse digestions have allowed to assigne to the conserved region a specific secondary structure. Mutational anaiysis has shown that this structure is important for conferring the cleavage phenotype to these three introns. Competition experiments show that the cleavage phenotype can be prevented by coinjection of excess amounts of homologous sequences.


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