Nucleic Acids Research, 1994, Vol. 22, No. 20 4082-4086
© 1994
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Characterization of RNA binding specificity of the Drosophila sex-lethal protein by in vitroligand selection
Department of Biology, Faculty of Science, Kobe University Rokkodai, Nadaku, Kobe 657, Japan
*To whom correspondence should be addressed
Received July 25, 1994. Revised August 30, 1994. Accepted August 30, 1994.
The Drosophila sex-lethal (Sxl) protein, a regulator of somatic sexual differentiation, is an RNA binding protein with two potential RNA recognition motifs (RRMs). It is thought to exert its function on splicing by binding to specific RNA sequences within Sxl and transformer (tra) pre-mRNAs. To examine the Sxl RNA binding specificity in detail, we performed in vitro selection and amplification of ligand RNAs from a random sequence pool on the basis of affinity with Sxl protein. After three cycles of selection and amplification, we cloned and sequenced 17 cDNAs corresponding to the RNAs selected in vitro. Sequencing showed that most of the RNAs selected contain polyuridine stretches surrounded by purine residues. In vitro binding analysis revealed that the sequences of the in vitro selected RNAs with relatively high affinity for Sxl show similarity to that of the Sxl- and tra- regulated acceptor regions, including the invariant AG sequence for splicing. These results suggest that Sxl recognizes and preferentially binds to a polyuridine stretch with a downstream AG sequence.
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