Isolation and characterization of the human tyrosine hydroxylase gene: identification of 5' alternative splice sites responsible for multiple mRNAs
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), Vol. 26:22
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
GENES
MOLECULAR BIOLOGY
TYROSINASE
DNA SEQUENCING
CARBON 14 COMPOUNDS
DNA-CLONING
GENETIC MAPPING
HYBRIDIZATION
MAN
MESSENGER-RNA
RATS
TRITIUM COMPOUNDS
TYROSINE
AMINO ACIDS
ANIMALS
CARBOXYLIC ACIDS
CLONING
ENZYMES
HYDROXY ACIDS
HYDROXYLASES
LABELLED COMPOUNDS
MAMMALS
MAPPING
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PRIMATES
RNA
RODENTS
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques