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 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 cross-linking in the nematode cuticle.
Department of Biology, University of San Diego, CA 92110, USA. cloer@acusd.edu
C M
CM
Loer
B
B
Davidson
J
J
Mckerrow
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics*; D018509:DNA, Helminth / Q000235:genetics; D015870:Gene Expression; D017930:Genes, Reporter; D007763:Lac Operon / Q000235:genetics; D008297:Male; D008969:Molecular Sequence Data; D010651:Phenylalanine Hydroxylase / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D014443:Tyrosine / Q000096:biosynthesis
D018509:DNA, Helminth; D014443:Tyrosine; D010651:Phenylalanine Hydroxylase