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Vol. 13, No. 20, pp. 2704-2712, October 15, 1999
Howard Hughes Medical Institute (HHMI), Department of Genetics, Duke
University Medical Center, Durham, North Carolina 27710 USA
Translational regulation of hunchback (hb) mRNA is
essential for posterior patterning of the Drosophila embryo.
This regulation is mediated by sequences in the 3'-untranslated
region of hb mRNA (the Nanos response elements or NREs), as
well as two trans-acting factors
Nanos and Pumilio. Pumilio
recognizes the NREs via a conserved binding motif. The mechanism of
Nanos action has not been clear. In this report we use protein-protein
and protein-RNA interaction assays in yeast and in vitro to show that
Nanos forms a ternary complex with the RNA-binding domain of Pumilio
and the NRE. Mutant forms of the NRE, Nos, and Pum that do not regulate
hb mRNA normally in embryos do not assemble normally into a
ternary complex. In particular, recruitment of Nos is dependent on
bases in the center of the NRE, on the carboxy-terminal
Cys/His domain of Nos, and on residues in the eighth
repeat of the Pum RNA-binding domain. These residues differ in a
closely related human protein that also binds to the NRE but cannot
recruit Drosophila Nos. Taken together, these findings suggest
models for how Nos and Pum collaboratively target hb mRNA. More
generally, they suggest that Pum-like proteins from other species may
also act by recruiting cofactors to regulate translation.
[Key Words: Drosophila; nanos; pumilio; RNA-binding protein; translational control]
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