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

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.

authors

Heinrichs V,Baker BS

doi

10.1073/pnas.94.1.115

subject

Has Abstract

pub_date

1997-01-07 00:00:00

pages

115-20

issue

1

eissn

0027-8424

issn

1091-6490

journal_volume

94

pub_type

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