Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene

G. A. Mitchell, J. E. Looney, L. C. Brody, G. Steel, M. Suchanek, J. F. Engelhardt, H. F. Willard, David Valle

Research output: Contribution to journalArticle

Abstract

Ornithine-δ-aminotranferase (OAT) is a nuclear-encoded, mitochondrial matrix enzyme which, in rat, is expressed as basal levels in most tissues but is induced in liver by high dietary protein and in kidney by estrogen and thyroxine administration. In man, the hereditary deficiency of OAT results in ornithine accumulation and the blinding disease gyrate atrophy of the choroid and retina. We cloned near full length rat and human liver OAT cDNAs and demonstrated OAT expression in a variety of tissues from each species. We mapped the human OAT structural gene to chromosome 10, cloned 40 kilobase pairs of genomic DNA containing the complete OAT structural gene, and determined its organization. It is 21 kilobase pairs in length, and contains 11 exons. Exon 2 has been absent from all cDNAs studied and was detected by homology to X-linked processed OAT pseudogenes. The 5'-flanking region of the OAT gene has features of house-keeping genes (GC enrichment and three Sp1 binding consensus sequences) and tissue-specific, inducible genes (TATA box-like element and two CCAAT boxes). A 22-base pair region of partial dyad symmetry containing homology to estrogen responsive elements overlaps the OAT transcription site. Another 5' sequence, GTATCCTGCCCTC, is homologous to sequences in the promoter regions of the genes of three urea cycle enzymes.

Original languageEnglish (US)
Pages (from-to)14288-14295
Number of pages8
JournalJournal of Biological Chemistry
Volume263
Issue number28
StatePublished - 1988

Fingerprint

Ornithine-Oxo-Acid Transaminase
Ornithine
Cloning
Organism Cloning
Complementary DNA
Genes
Tissue
Liver
Rats
Exons
Estrogens
Gyrate Atrophy
Chromosomes, Human, Pair 10
TATA Box
Pseudogenes
Dietary Proteins
5' Flanking Region
Essential Genes
Consensus Sequence
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mitchell, G. A., Looney, J. E., Brody, L. C., Steel, G., Suchanek, M., Engelhardt, J. F., ... Valle, D. (1988). Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene. Journal of Biological Chemistry, 263(28), 14288-14295.

Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene. / Mitchell, G. A.; Looney, J. E.; Brody, L. C.; Steel, G.; Suchanek, M.; Engelhardt, J. F.; Willard, H. F.; Valle, David.

In: Journal of Biological Chemistry, Vol. 263, No. 28, 1988, p. 14288-14295.

Research output: Contribution to journalArticle

Mitchell, GA, Looney, JE, Brody, LC, Steel, G, Suchanek, M, Engelhardt, JF, Willard, HF & Valle, D 1988, 'Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene', Journal of Biological Chemistry, vol. 263, no. 28, pp. 14288-14295.
Mitchell GA, Looney JE, Brody LC, Steel G, Suchanek M, Engelhardt JF et al. Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene. Journal of Biological Chemistry. 1988;263(28):14288-14295.
Mitchell, G. A. ; Looney, J. E. ; Brody, L. C. ; Steel, G. ; Suchanek, M. ; Engelhardt, J. F. ; Willard, H. F. ; Valle, David. / Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 28. pp. 14288-14295.
@article{b18ab3c2d9fb42d8a16deda78f32634a,
title = "Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene",
abstract = "Ornithine-δ-aminotranferase (OAT) is a nuclear-encoded, mitochondrial matrix enzyme which, in rat, is expressed as basal levels in most tissues but is induced in liver by high dietary protein and in kidney by estrogen and thyroxine administration. In man, the hereditary deficiency of OAT results in ornithine accumulation and the blinding disease gyrate atrophy of the choroid and retina. We cloned near full length rat and human liver OAT cDNAs and demonstrated OAT expression in a variety of tissues from each species. We mapped the human OAT structural gene to chromosome 10, cloned 40 kilobase pairs of genomic DNA containing the complete OAT structural gene, and determined its organization. It is 21 kilobase pairs in length, and contains 11 exons. Exon 2 has been absent from all cDNAs studied and was detected by homology to X-linked processed OAT pseudogenes. The 5'-flanking region of the OAT gene has features of house-keeping genes (GC enrichment and three Sp1 binding consensus sequences) and tissue-specific, inducible genes (TATA box-like element and two CCAAT boxes). A 22-base pair region of partial dyad symmetry containing homology to estrogen responsive elements overlaps the OAT transcription site. Another 5' sequence, GTATCCTGCCCTC, is homologous to sequences in the promoter regions of the genes of three urea cycle enzymes.",
author = "Mitchell, {G. A.} and Looney, {J. E.} and Brody, {L. C.} and G. Steel and M. Suchanek and Engelhardt, {J. F.} and Willard, {H. F.} and David Valle",
year = "1988",
language = "English (US)",
volume = "263",
pages = "14288--14295",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

TY - JOUR

T1 - Human ornithine-δ-aminotransferase. cDNA cloning and analysis of the structural gene

AU - Mitchell, G. A.

AU - Looney, J. E.

AU - Brody, L. C.

AU - Steel, G.

AU - Suchanek, M.

AU - Engelhardt, J. F.

AU - Willard, H. F.

AU - Valle, David

PY - 1988

Y1 - 1988

N2 - Ornithine-δ-aminotranferase (OAT) is a nuclear-encoded, mitochondrial matrix enzyme which, in rat, is expressed as basal levels in most tissues but is induced in liver by high dietary protein and in kidney by estrogen and thyroxine administration. In man, the hereditary deficiency of OAT results in ornithine accumulation and the blinding disease gyrate atrophy of the choroid and retina. We cloned near full length rat and human liver OAT cDNAs and demonstrated OAT expression in a variety of tissues from each species. We mapped the human OAT structural gene to chromosome 10, cloned 40 kilobase pairs of genomic DNA containing the complete OAT structural gene, and determined its organization. It is 21 kilobase pairs in length, and contains 11 exons. Exon 2 has been absent from all cDNAs studied and was detected by homology to X-linked processed OAT pseudogenes. The 5'-flanking region of the OAT gene has features of house-keeping genes (GC enrichment and three Sp1 binding consensus sequences) and tissue-specific, inducible genes (TATA box-like element and two CCAAT boxes). A 22-base pair region of partial dyad symmetry containing homology to estrogen responsive elements overlaps the OAT transcription site. Another 5' sequence, GTATCCTGCCCTC, is homologous to sequences in the promoter regions of the genes of three urea cycle enzymes.

AB - Ornithine-δ-aminotranferase (OAT) is a nuclear-encoded, mitochondrial matrix enzyme which, in rat, is expressed as basal levels in most tissues but is induced in liver by high dietary protein and in kidney by estrogen and thyroxine administration. In man, the hereditary deficiency of OAT results in ornithine accumulation and the blinding disease gyrate atrophy of the choroid and retina. We cloned near full length rat and human liver OAT cDNAs and demonstrated OAT expression in a variety of tissues from each species. We mapped the human OAT structural gene to chromosome 10, cloned 40 kilobase pairs of genomic DNA containing the complete OAT structural gene, and determined its organization. It is 21 kilobase pairs in length, and contains 11 exons. Exon 2 has been absent from all cDNAs studied and was detected by homology to X-linked processed OAT pseudogenes. The 5'-flanking region of the OAT gene has features of house-keeping genes (GC enrichment and three Sp1 binding consensus sequences) and tissue-specific, inducible genes (TATA box-like element and two CCAAT boxes). A 22-base pair region of partial dyad symmetry containing homology to estrogen responsive elements overlaps the OAT transcription site. Another 5' sequence, GTATCCTGCCCTC, is homologous to sequences in the promoter regions of the genes of three urea cycle enzymes.

UR - http://www.scopus.com/inward/record.url?scp=0023785183&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023785183&partnerID=8YFLogxK

M3 - Article

C2 - 3170546

AN - SCOPUS:0023785183

VL - 263

SP - 14288

EP - 14295

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -