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Proc Natl Acad Sci U S A
1996 Oct 29;9322:12315-20. doi: 10.1073/pnas.93.22.12315.
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Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and the gut.
Hintermann E
,
Grieder NC
,
Amherd R
,
Brodbeck D
,
Meyer UA
.
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In insects, neurotransmitter catabolism, melatonin precursor formation, and sclerotization involve arylalkylamine N-acetyltransferase (aaNAT, EC 2.3.1.87) activity. It is not known if one or multiple aaNAT enzymes are responsible for these activities. We recently have purified an aaNAT from Drosophila melanogaster. Here, we report the cloning of the corresponding aaNAT cDNA (aaNAT1) that upon COS cell expression acetylates dopamine, tryptamine, and the immediate melatonin precursor serotonin. aaNAT1 represents a novel gene family unrelated to known acetyl-transferases, except in two weakly conserved amino acid motifs. In situ hybridization studies of aaNAT1 mRNA in embryos reveal hybridization signals in the brain, the ventral cord, the gut, and probably in oenocytes, indicating a broad tissue distribution of aaNAT1 transcripts. Moreover, in day/ night studies we demonstrate a diurnal rhythm of melatonin concentration without a clear-cut change in aaNAT1 mRNA levels. The data suggest that tissue-specific regulation of aaNAT1 may be associated with different enzymatic functions and do not exclude the possibility of additional aaNAT genes.
FIG. 5. Genomic Southern blot analysis in different vertebrate species. Genomic DNA from different species was digested with BamHI (Left)
or XbaI (Right), except for D, in which both lanes reflect XbaI digestion. (A) Xenopus, 757-bp aaNAT1 probe, 30% formamide. (B) Carp, 757-bp
probe, 25% formamide. (C) Chicken, 3'-probe, 30% formamide. (D) Mouse (Left) and human (Right), 757-bp probe, 43% formamide.
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