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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

In vivo analysis of the functional domains of the Drosophila splicing regulator RBP1.

The Drosophila splicing factor RBP1 participates together with TRA and TRA-2 in the regulation of alternative splicing of doublesex (dsx) pre-mRNA. It does so by recognizing RBP1 RNA target sequences in the dsx pre-mRNA. RBP1 belongs to the Ser-Arg-rich (SR) protein family of splicing factors, which have in common a N-terminal RNA recognition motif-type RNA binding domain, a Gly-rich region, and a C-terminal SR domain. Using a tissue culture transfection assay, we demonstrate that the Gly residues within the Gly-rich domain, the ribonucleoprotein motifs within the RNA recognition motif RNA binding domain, and the SR domain are required for regulation of dsx splicing by RBP1 in vivo. Furthermore, using a two-hybrid system, we show protein-protein interactions between RBP1 and itself and between RBP1 and TRA-2. The SR domain and the Gly residues within the Gly-rich domain of RBP1 were found to be involved in these protein-protein interactions. Our results suggest that RBP1 and TRA-2 function in regulation of dsx splicing by forming a complex.[1]

References

  1. In vivo analysis of the functional domains of the Drosophila splicing regulator RBP1. Heinrichs, V., Baker, B.S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
 
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