Molecular Genetics of Tyrosine Hydroxylase

Mallet, Jacques; Bérod, Anne; Blanot, Francois; Boni, Claudette; Buda, M.; Biguet, Nicole Faucon; Grima, Brigitte; Horellou, Philippe; Julien, Jean‐François; Lamouroux, Annie; Powell, Jerry S.

doi:10.1007/978-1-4613-2321-1_6

Cited by 6 publications

(1 citation statement)

References 28 publications

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“…It a 26 bp poly(A) tail. Primer extension and nuclease appears unlikely, therefore, that the size difference we protection experiments have shown that the human and observe by SDS-PAGE can be attributed to species-sperat TH mRNAs contain 29 and 35 nucleotides of 5' cific differences in posttranslational modification of the untranslated region, respectively (Mallet et al, 1986;enzyme. Interestingly, all of the amino acid residues Grima et al, 1987;Harrington et al, 1987). Assuming a absent from the cow protein are missing from an alanineregion of similar length for bovine TH mRNA, the rich region in the N-terminal portion of the rat enzyme XbTH1_5 clone lacks approximately 15-20 residues at its (amino acid residues 51-68 in the rat).…”

Section: Lack Of Sequence Homology Between Th and Phenylethanolamine mentioning

confidence: 98%

Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products

D’Mello

Weisberg

Stachowiak

et al. 1988

J of Neuroscience Research

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Investigations into the structure and mechanisms regulating the expression of the genes involved in catecholamine biosynthesis have led to the isolation of a cDNA coding for bovine adrenal tyrosine hydroxylase (TH). The 1,722 bp cDNA contains the complete coding sequence and 3' untranslated region of the TH mRNA. The nucleotide sequence of the cDNA and the deduced amino acid sequence were compared to those reported for rat and human TH. Bovine TH shares 85% and 84% amino acid sequence identity with that of rat and human TH, respectively. Alignment of the amino acid sequences of rat, bovine, and human TH reveals that 79% of the residues are identical in all three species, indicating a strong evolutionary conservation of enzyme structure. Moreover, three of the four putative phosphorylation sites located in the N-terminal region of TH are conserved in these animal species. There are, however, some interspecies differences in TH gene products. The 3' untranslated region of bovine TH mRNA is 56 and 97 nucleotides shorter than rat and human TH mRNA, respectively. Additionally, the bovine protein is 7 and 6 amino acids smaller than its rat and human homologues. All of the absent amino acid residues of bovine TH are missing from an alanine-rich region in the N-terminal portion of the rat and human proteins (amino acids 51-68). Comparison of the size of bovine and rat TH mRNA and protein by northern blot and immunoblot analyses yielded differences consistent with those predicted from the nucleotide sequence data.

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Section: Lack Of Sequence Homology Between Th and Phenylethanolamine mentioning

confidence: 98%

Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products

D’Mello

Weisberg

Stachowiak

et al. 1988

J of Neuroscience Research

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A fine-structure deletion map of human chromosome 11p: Analysis of J1 series hybrids

Gläser

Housman

Lewis

et al. 1989

Somat Cell Mol Genet

123

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Deletion analysis offers a powerful alternative to linkage and karyotypic approaches for human chromosome mapping. A panel of deletion hybrids has been derived by mutagenizing J1, a hamster cell line that stably retains chromosome 11 as its only human DNA, and selecting for loss of MIC1, a surface antigen encoded by a gene in band 11p13. A unique, self-consistent map was constructed by analyzing the pattern of marker segregation in 22 derivative cells lines; these carry overlapping deletions of 11p13, but selectively retain a segment near the 11p telomere. The map orders 35 breakpoints and 36 genetic markers, including 3 antigens, 2 isozymes, 12 cloned genes, and 19 anonymous DNA probes. The deletions span the entire short arm, dividing it into more than 20 segments and define a set of reagents that can be used to rapidly locate any newly identified marker on 11p, with greatest resolution in the region surrounding MIC1. The approach we demonstrate can be applied to map any mammalian chromosome. To test the gene order, we examined somatic cell hybrids from five patients, whose reciprocal translocations bisect band 11p13; these include two translocations associated with familial aniridia and two with acute T-cell leukemia. In each patient, the markers segregate in telomeric and centromeric groups as predicted by the deletion map. These data locate the aniridia gene (AN2) and a recurrent T-cell leukemia breakpoint (TCL2) in the marker sequence, on opposite sides of MIC1. To provide additional support, we have characterized the dosage of DNA markers in a patient with Beckwith-Wiedemann syndrome and an 11p15-11pter duplication. Our findings suggest the following gene order: TEL - (HRAS1, MER2, CTSD, TH/INS/IGF2, H19, D11S32) - (RRM1, D11S1, D11S25, D11S26) - D11S12 - (HBBC, D11S30) - D11S20 - (PTH, CALC) - (LDHA, SAA, TRPH, D11S18, D11S21) - D11S31 - D11S17 - HBVS1 - (FSHB, D11S16) - AN2 - MIC1 - TCL2 - delta J - CAT - MIC4 - D11S9 - D11S14 - ACP2 - (D11S33, 14L) - CEN. We have used the deletion map to show the distribution on 11p of two centromeric repetitive elements and the low-order interspersed repeat A36Fc. Finally, we provide evidence for an allelic segregation event in the hamster genome that underlies the stability of chromosome 11 in J1. The deletion map provides a basis to position hereditary disease loci on 11p, to distinguish the pattern of recessive mutations in different forms of cancer and, since many of these genes have been mapped in other mammalian species, to study the evolution of a conserved syntenic group.

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A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics

Grima

Lamouroux

Boni

et al. 1987

Nature

350

206

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Catecholaminergic systems in discrete regions of the brain are thought to be important in affective psychoses, learning and memory, reinforcement and sleep-wake cycle regulation. Tyrosine hydroxylase (TH) is the first enzyme in the pathway of catecholamine synthesis. Its importance is reflected in the diversity of the mechanisms that have been described which control its activity; TH levels vary both during development and as a function of the activity of the nervous system. Recently, we deduced the complete amino-acid sequence of rat TH from a complementary DNA clone encoding a functional enzyme. Here we demonstrate that, in man, TH molecules are encoded by at least three distinct messenger RNAs. The expression of these mRNAs varies in different parts of the nervous system. The sequence differences observed are confined to the 5' termini of the messengers and involve alternative splicing events. This variation has clear functional consequences for each putative form of the enzyme and could represent a novel means of regulating catecholamine levels in normal and pathological neurons.

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Molecular Genetics of Tyrosine Hydroxylase

Cited by 6 publications

References 28 publications

Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products

Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products

A fine-structure deletion map of human chromosome 11p: Analysis of J1 series hybrids

A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics

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