Nucleic Acids Research, Vol 27, Issue 11 2377-2386, Copyright © 1999 by Oxford University Press
E Labourier, E Allemand, S Brand, M Fostier, J Tazi and HM Bourbon
The Drosophila repressor splicing factor 1 (RSF1) comprises an N- terminal
RNA-binding region and a C-terminal domain rich in glycine, arginine and
serine residues, termed the GRS domain. Recently, RSF1 has been shown to
antagonize splicing factors of the serine/arginine-rich (SR) family and it
is, therefore, expected to play a role in processing of a subset of
Drosophila pre-mRNAs through specific interactions with RNA. To investigate
the RNA-binding specificity of RSF1, we isolated RSF1-binding RNAs using an
in vitro selection approach. We have identified two RNA target motifs
recognized by RSF1, designated A (CAACGACGA)- and B (AAACGCGCG)-type
sequences. We show here that the A- type cognate sequence behaves as an SR
protein-dependent exonic splicing enhancer. Namely, three copies of the
A-type ligand bind SR proteins, stimulate the efficiency of splicing of
reporter pre-mRNAs several fold and lead to inclusion of a short internal
exon both in vitro and in vivo. However, three copies of a B-type ligand
were much less active. The finding that RSF1 acts as a potent repressor of
pre- mRNA splicing in vitro led us to propose that the equilibrium between
a limited number of structurally-related general splicing activators or
repressors, competing for common or promiscuous binding sites, may be a
major determinant of the underlying mechanisms controlling many alternative
pre-mRNA process-ing events.
ARTICLES
Recognition of exonic splicing enhancer sequences by the Drosophila splicing repressor RSF1
Institut de Genetique Moleculaire, UMR5535 du CNRS, 1919 Route de Mende, F34293 Montpellier Cedex 5, France.
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