Evolutionary conservation of the vertebrate Ah (dioxin) receptor: amplification and sequencing of the PAS domain of a teleost Ah receptor cDNA.
The PAS domain of a teleost Ah receptor was amplified using reverse transcription-PCR with degenerate primers containing inosine. The deduced amino acid sequence of the amplified cDNA fragment was 62-64% identical with the PAS domains of mammalian Ah receptors. These data demonstrate the homology of Ah receptors in mammals and fish, and reveal regions of this protein that are highly conserved between these diverse vertebrate groups.
Hahn
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Biology Department, Woods Hole Oceanographic Institution, MA 02543-1049, USA.
Karchner
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D017124:Conserved Sequence; D017931:DNA Primers; D018076:DNA, Complementary; D015870:Gene Expression; D006801:Humans; D007695:Killifishes / Q000235:genetics*; D008297:Male; D008322:Mammals / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D051381:Rats; D018336:Receptors, Aryl Hydrocarbon / Q000096:biosynthesis* / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D018076:DNA, Complementary; D018336:Receptors, Aryl Hydrocarbon