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Vol. 13, No. 6, pp. 740-753, March 15, 1999
1 Institut de Génétique Moléculaire,
Centre National de la Recherche Scientifique (CNRS), F34293 Montpellier
Cedex 5, France; 2 Centre de Biologie du Développement,
CNRS, Université Paul Sabatier, F31062 Toulouse, France
Specific recognition of splice sites within metazoan mRNA precursors
(pre-mRNAs) is a potential stage for gene regulation by alternative
splicing. Splicing factors of the SR protein family play a major role
in this regulation, as they are required for early recognition of
splice sites during spliceosome assembly. Here, we describe the
characterization of RSF1, a splicing repressor isolated from
Drosophila, that functionally antagonizes SR proteins. Like the
latter, RSF1 comprises an amino-terminal RRM-type RNA-binding domain,
whereas its carboxy-terminal part is enriched in glycine (G), arginine
(R), and serine (S) residues (GRS domain). RSF1 induces a
dose-sensitive inhibition of splicing for several reporter pre-mRNAs,
an inhibition that occurs at the level of early splicing complexes
formation. RSF1 interacts, through its GRS domain, with the RS domain
of the SR protein SF2/ASF and prevents the latter from
cooperating with the U1 small nuclear ribonucleoprotein particle (U1
snRNP) in binding pre-mRNA. Furthermore, overproduction of RSF 1 in the
fly rescues several developmental defects caused by overexpression of
the splicing activator SR protein B52/ SRp55. Therefore,
RSF1 may correspond to the prototypical member of a novel family of
general splicing repressors that selectively antagonize the effect of
SR proteins on 5' splice-site recognition.
[Key Words: pre-mRNA splicing; RNA-binding proteins; SF2/ASF; U1 snRNP; RSF1; B52/SRp55]
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