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© Research
Publication : Genes & development

Antagonism between RSF1 and SR proteins for both splice-site recognition in vitro and Drosophila development

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Genes & development - 15 Mar 1999

Labourier E, Bourbon HM, Gallouzi IE, Fostier M, Allemand E, Tazi J

Link to Pubmed [PMID] – 10090730

Genes Dev. 1999 Mar;13(6):740-53

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.

http://www.ncbi.nlm.nih.gov/pubmed/10090730