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Gene Review

Rsf1  -  Repressor splicing factor 1

Drosophila melanogaster

Synonyms: CG5655, Dmel\CG5655, RNA-binding protein Rox21, RNA-binding protein Rsf1, ROX21, ...
 
 
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High impact information on Rsf1

  • 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) [1].
  • Using the yeast model system in which nuclear import of Drosophila SR proteins and RSF1 is impaired, we demonstrate that complementation with dTRN-SR is sufficient to target these proteins to the nucleus [2].
  • Far Western experiments established that the RS domain of SR proteins and the GRS domain of RSF1 are required for the direct interaction with dTRN-SR, an interaction that can be modulated by phosphorylation [2].
  • 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 [3].
  • Recognition of exonic splicing enhancer sequences by the Drosophila splicing repressor RSF1 [3].
 

Biological context of Rsf1

References

  1. Antagonism between RSF1 and SR proteins for both splice-site recognition in vitro and Drosophila development. Labourier, E., Bourbon, H.M., Gallouzi, I.E., Fostier, M., Allemand, E., Tazi, J. Genes Dev. (1999) [Pubmed]
  2. A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1. Allemand, E., Dokudovskaya, S., Bordonné, R., Tazi, J. Mol. Biol. Cell (2002) [Pubmed]
  3. Recognition of exonic splicing enhancer sequences by the Drosophila splicing repressor RSF1. Labourier, E., Allemand, E., Brand, S., Fostier, M., Tazi, J., Bourbon, H.M. Nucleic Acids Res. (1999) [Pubmed]
 
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