A Phenylalanine Hydroxylase Gene from the Nematode C. Elegans is Expressed in the Hypodermis

We have identified an aromatic amino acid hydroxylase gene from the nematode C. elegans that likely encodes the worm phenylalanine hydroxylase (PheH). The predicted amino acid sequence is most similar to that of other PheH and TrpH proteins. Reporter gene fusions and staining with an antibody to mam...

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Bibliographic Details
Published in:Journal of neurogenetics 1999-01, Vol.13 (3), p.157-180
Main Authors: Loer, Curtis M., Davidson, Brian, McKerrow, James
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Aromatic amino acid hydroxylase
Base Sequence
Caenorhabditis elegans - enzymology
Caenorhabditis elegans - genetics
cuticle
DNA, Helminth - genetics
Gene Expression
Genes, Reporter
Lac Operon - genetics
Male
Molecular Sequence Data
Phenylalanine Hydroxylase - genetics
Phenylalanine Hydroxylase - metabolism
Phenylalanine Hydroxylase - physiology
pterin-dependent monooxygenase
tryptophan hydroxylase
Tyrosine - biosynthesis
tyrosine cross-linking
tyrosine hydroxylase
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Summary:We have identified an aromatic amino acid hydroxylase gene from the nematode C. elegans that likely encodes the worm phenylalanine hydroxylase (PheH). The predicted amino acid sequence is most similar to that of other PheH and TrpH proteins. Reporter gene fusions and staining with an antibody to mammalian PheH indicate the gene is expressed in hypodermal cells. A fusion protein expressed in bacteria can convert phenylalanine to tyrosine, and, to a lesser extent, tryptophan to 5-hydroxytryptophan. We hypothesize that the protein is necessary to produce additional tyrosine for protein crosslinking in the nematode cuticle.
ISSN:0167-7063
1563-5260
DOI:10.3109/01677069909083472