Nucleic Acids Research, Vol 26, Issue 11 2625-2637, Copyright © 1998 by Oxford University Press
M Samuels, G Deshpande and P Schedl
The Drosophila sex determination gene Sex-lethal (Sxl) controls its own
expression, and the expression of downstream target genes such as
transformer , by regulating pre-mRNA splicing and mRNA translation. Sxl
codes an RNA-binding protein that consists of an N-terminus of
approximately 100 amino acids, two 90 amino acid RRM domains, R1 and R2,
and an 80 amino acid C-terminus. In the studies reported here we have
examined the functional properties of the different Sxl protein domains in
RNA binding and in protein:protein interactions. The two RRM domains are
responsible for RNA binding. Specificity in the recognition of target RNAs
requires both RRM domains, and proteins which consist of the single domains
or duplicated domains have anomalous RNA recognition properties. Moreover,
the length of the linker between domains can affect RNA recognition
properties. Our results indicate that the two RRM domains mediate Sxl:Sxl
protein interactions, and that these interactions probably occur both in
cis and trans. We speculate that cis interactions between R1 and R2 play a
role in RNA recognition by the Sxl protein, while trans interactions
stabilize complex formation on target RNAs that contain two or more closely
spaced binding sites. Finally, we show that the interaction of Sxl with the
snRNP protein Snf is mediated by the R1 RRM domain.
ARTICLES
Activities of the Sex-lethal protein in RNA binding and protein:protein interactions
Department of Molecular Biology, Princeton University, Princeton, NJ 08540, USA.
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