Literature DB >> 1996964

Cloning, sequencing and expression of cDNA for chick liver haem oxygenase. Comparison of avian and mammalian cDNAs and deduced proteins.

C O Evans1, J F Healey, Y Greene, H L Bonkovsky.   

Abstract

A cDNA from a chick liver library that encodes for haem oxygenase has been cloned and sequenced. Positive clones were identified with monospecific antibodies to the purified enzyme from chick liver and a cDNA of rat haem oxygenase-1. The length of the cDNA is 1258 bases. An open reading frame of 888 bases was identified by comparison of nucleotide and amino acid sequences with those previously identified for haem oxygenase of mammalian or avian origin. The protein corresponding to this fragment of DNA is composed of 296 amino acid residues and has a molecular mass of 33,509 Da, which is similar to that previously estimated for haem oxygenase purified from chick liver. Unequivocal identification of this clone as that complementary to haem oxygenase was provided by (a) comparison of amino acid compositions and partial sequences with those previously established for the purified enzyme, (b) comparison with nucleotide and amino acid sequences for haem oxygenase from rat and human sources and (c) expression in Escherichia coli with production of high levels of mRNA, protein and haem oxygenase activity after exposure of the transfected bacteria to isopropyl beta-D-thiogalactopyranoside (IPTG). Overall, the similarity of chick haem oxygenase to rat and human haem oxygenase (nucleotides 66% and amino acids 62%) is moderately high. The region between proline-129 and alanine-157 is identical in all three enzymes, including histidine-135, which is proposed to play a key role in binding the substrate haem at the active centre of the enzyme. Northern blots also show that treatment of chicks with CdCl2, a potent inducer of haem oxygenase, results in increases in 1.65-1.70 kb mRNA, which hybridizes selectively to the full-length cDNA or to a synthetic 24-base oligonucleotide with sequence identical to that of a portion of the haem oxygenase cDNA. These results suggest that Cd-dependent induction of haem oxygenase is due to increased transcription of the gene or stabilization of its message.

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Year:  1991        PMID: 1996964      PMCID: PMC1149814          DOI: 10.1042/bj2730659

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  37 in total

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3.  Regulation of hepatic haem metabolism. Disparate mechanisms of induction of haem oxygenase by drugs and metals.

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Review 4.  The physiological significance of heme oxygenase.

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Journal:  Int J Biochem       Date:  1988

Review 5.  Role of cytochrome P-450 in porphyria caused by halogenated aromatic compounds.

Authors:  H L Bonkovsky; P R Sinclair; W J Bement; R W Lambrecht; J F Sinclair
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Authors:  J W Hamilton; W J Bement; P R Sinclair; J F Sinclair; K E Wetterhahn
Journal:  Biochem J       Date:  1988-10-01       Impact factor: 3.857

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Authors:  M M McKinney; A Parkinson
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8.  Immunochemical detection of different isoenzymes of cytochrome P-450 induced in chick hepatocyte cultures.

Authors:  P Sinclair; J Frezza; J Sinclair; W Bement; S Haugen; J Healey; H Bonkovsky
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Review 9.  Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications.

Authors:  M D Maines
Journal:  FASEB J       Date:  1988-07       Impact factor: 5.191

10.  Lambda ZAP: a bacteriophage lambda expression vector with in vivo excision properties.

Authors:  J M Short; J M Fernandez; J A Sorge; W D Huse
Journal:  Nucleic Acids Res       Date:  1988-08-11       Impact factor: 16.971

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  3 in total

1.  Upstream regulatory elements in chick heme oxygenase-1 promoter: a study in primary cultures of chick embryo liver cells.

Authors:  T H Lu; Y Shan; J Pepe; R W Lambrecht; H L Bonkovsky
Journal:  Mol Cell Biochem       Date:  2000-06       Impact factor: 3.396

2.  The heme oxygenase gene (pbsA) in the red alga Rhodella violacea is discontinuous and transcriptionally activated during iron limitation.

Authors:  C Richaud; G Zabulon
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-14       Impact factor: 11.205

3.  Immunochemical studies of haem oxygenase. Preparation and characterization of antibodies to chick liver haem oxygenase and their use in detecting and quantifying amounts of haem oxygenase protein.

Authors:  Y J Greene; J F Healey; H L Bonkovsky
Journal:  Biochem J       Date:  1991-11-01       Impact factor: 3.857

  3 in total

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