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Volume 16, Number 12,
Issue of June 15, 1996
pp. 3900-3911
Copyright ©1996 Society for Neuroscience
Characterization of Drosophila Tyramine  -Hydroxylase
Gene and Isolation of Mutant Flies Lacking Octopamine
Received Nov. 14, 1995; revised March 27, 1996; accepted March 29, 1996.
Maria Monastirioti1,
Charles E. Linn, Jr.2, and
Kalpana White1
1 Biology Department and Volen National Center for
Complex Systems, Brandeis University, Waltham, Massachusetts 02254, and
2 Entomology Department, New York State Agricultural
Experiment Station, Cornell University, Geneva, New York 14456
Octopamine is likely to be an important neuroactive molecule in
invertebrates. Here we report the molecular cloning of the
Drosophila melanogaster gene, which encodes tyramine
 -hydroxylase (TBH), the enzyme that catalyzes the last step in
octopamine biosynthesis. The deduced amino acid sequence of the encoded
protein exhibits 39% identity to the evolutionarily related mammalian
dopamine -hydroxylase enzyme. We generated a polyclonal antibody
against the protein product of Th gene, and we
demonstrate that the TBH expression pattern is remarkably similar to
the previously described octopamine immunoreactivity in
Drosophila. We further report the creation of null mutations
at the Th locus, which result in complete absence of TBH
protein and blockage of the octopamine biosynthesis.
Th-null flies are octopamine-less but survive to
adulthood. They are normal in external morphology, but the females are
sterile, because although they mate, they retain fully developed eggs.
Finally, we demonstrate that this defect in egg laying is associated
with the octopamine deficit, because females that have retained eggs
initiate egg laying when transferred onto octopamine-supplemented
food.
Key words:
cloning of Tyramine -hydroxylase;
TBH-immunocytochemistry;
Dopamine -hydroxylase;
octopamine-null mutant;
egg-laying behavior;
Drosophila
neurogenetics
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