Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Heinrichs V,Baker BSdoi
10.1073/pnas.94.1.115subject
Has Abstractpub_date
1997-01-07 00:00:00pages
115-20issue
1eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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