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Isolation and characterization of the human tyrosine hydroxylase gene: identification of 5' alternative splice sites responsible for multiple mRNAs

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00396a007· OSTI ID:5515641
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A full-length genomic clone for human tyrosine hydroxylase (L-tyrosine, tetrahydropteridine:oxygen oxidoreductase, EC 1.14.16.2) has been isolated. A human brain genomic library constructed in EMBL3 was screened by using a rat cDNA for tyrosine hydroxylase as a probe. Out of one million recombinant phage, one clone was identified that hybridized to both 5' and 3' rat cDNA probes. Restriction endonuclease mapping, Southern blotting, and sequence analysis revealed that, like its rodent counterpart, the human gene is single copy, contains 13 primary exons, and spans approximately 8 kilobases (kb). In contrast to the rat gene, human tyrosine hydroxylase undergoes alternative RNA processing within intron 1, generating at least three distinct mRNAs. A comparison of the human tyrosine hydroxylase and phenylalanine hydroxylase genes indicates that although both probably evolved from a common ancestral gene, major changes in the size of introns have occurred since their divergence.
Research Organization:
Washington Univ. School of Medicine, St. Louis, MO
OSTI ID:
5515641
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:22; ISSN BICHA
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMALS
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CLONING
DNA SEQUENCING
DNA-CLONING
ENZYMES
GENES
GENETIC MAPPING
HYBRIDIZATION
HYDROXY ACIDS
HYDROXYLASES
LABELLED COMPOUNDS
MAMMALS
MAN
MAPPING
MESSENGER-RNA
MOLECULAR BIOLOGY
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PRIMATES
RATS
RNA
RODENTS
STRUCTURAL CHEMICAL ANALYSIS
TRITIUM COMPOUNDS
TYROSINASE
TYROSINE
VERTEBRATES