The Drosophila proteins Transformer (Tra) and Transformed (Tra2) regul
ate the sex-specific alternative splicing of Drosophila doublesex (dsx
) pre-mRNA by specifically binding to a splicing enhancer (dsx repeat
element; dsxRE) located 300 nucleotides (nt) downstream from a female-
specific 3' splice site. In this paper we show that the dsxRE can func
tion as a Tra and Tra2-independent splicing enhancer in vitro when loc
ated within 150 nucleotides of the 3' splice site. Based on the relati
ve levels of SR proteins that bind stably to the dsxRE in the presence
or absence of Tra and Tra2, we propose that the constitutive splicing
activity of the dsxRE is mediated by its weak interactions with SR pr
oteins and possibly other general splicing factors. In contrast, Tra a
nd Tra2 allow the dsxRE to function at a distance from the intron by s
tabilizing the interactions between these proteins and the dsxRE.