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J. Biol. Chem., Vol. 265, Issue 4, 1913-1918, Feb, 1990
L Shemshedini, M Lanoue and TG Wilson
The larval fat body of newly eclosed adults of Drosophila melanogaster was
found to contain a single major binding protein specific for juvenile
hormone (JH). Binding to this protein was saturable, of high affinity, and
specific for JH III. The protein has a subunit molecular weight (Mr) of
85,000, as determined by photoaffinity labeling. The same or similar
JH-binding protein was found in larval fat body and cuticle of third instar
larvae and in male accessory glands and heads of newly eclosed adults. It
was not found in several other tissues in adults. Male accessory gland
cytosol from wild-type flies was found to contain a single binder with a
dissociation constant (KD) of 6.7 nM for JH III; a binder in similar
preparations from the methoprene-tolerant (Met) mutant had a KD value
6-fold higher. JH III stimulated protein synthesis in glands cultured in
vitro, but this effect was reduced in Met flies as compared to wild-type
flies, establishing a correlation between JH binding and biological
activity of the hormone. In addition, glandular protein accumulation during
the first 2 days of adult development was less in Met flies than in
wild-type flies. These results strongly suggest that the binding protein we
have identified mediates this JH effect in male accessory glands and thus
is acting as a JH receptor.
Evidence for a juvenile hormone receptor involved in protein synthesis in Drosophila melanogaster
Department of Zoology, University of Vermont, Burlington 05405.
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