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Gene Review

ho1  -  heme oxygenase

Synechocystis sp. PCC 6803

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Disease relevance of ho1

  • This gene, named ho1, was cloned and expressed in Escherichia coli under the control of the lacZ promoter [1].
  • Two paralogs of ho (ho1 and ho2) have been identified in the genome of the cyanobacterium, Synechocystis sp. PCC 6803 [2].
  • This construct was placed in a binary plasmid vectorcontaining a kanamycin resistance marker and a cauliflower mosaic virus 35S promoter to control expression of the chimeric oli-ho1 gene and used to transform A. thaliana hy1 plants [3].
  • In cyanobacteria, red algae, and cryptophyceae, HO is a key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae [4].

High impact information on ho1

  • The phytobilin chromophores of phycobiliproteins and phytochromes are biosynthesized from heme in a pathway that begins with the opening of the tetrapyrrole macrocycle of protoheme to form biliverdin IX alpha, in a reaction catalyzed by heme oxygenase [1].
  • The open reading frame of ho1 was fused in frame with a chloroplast transit peptide-encoding sequence from the oli gene of Antirrhinum majus [3].
  • Carbon monoxide (CO) is produced during the heme catabolism by heme oxygenase [5].
  • An efficient bacterial expression system of cyanobacterium Synechocystis sp. PCC 6803 heme oxygenase gene, ho-1, has been constructed, using a synthetic gene [6].
  • Two isoforms of a heme oxygenase gene, ho1 and ho2, with 51% identity in amino acid sequence have been identified in the cyanobacterium Synechocystis sp. PCC 6803 [7].

Analytical, diagnostic and therapeutic context of ho1


  1. Phytobilin biosynthesis: cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803. Cornejo, J., Willows, R.D., Beale, S.I. Plant J. (1998) [Pubmed]
  2. Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme. Sugishima, M., Hagiwara, Y., Zhang, X., Yoshida, T., Migita, C.T., Fukuyama, K. Biochemistry (2005) [Pubmed]
  3. Phytobilin biosynthesis: the Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thalianna hy1 mutant. Willows, R.D., Mayer, S.M., Foulk, M.S., DeLong, A., Hanson, K., Chory, J., Beale, S.I. Plant Mol. Biol. (2000) [Pubmed]
  4. The heme oxygenase gene (pbsA) in the red alga Rhodella violacea is discontinuous and transcriptionally activated during iron limitation. Richaud, C., Zabulon, G. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Evidence for the hydrophobic cavity of heme oxygenase-1 to be a CO-trapping site. Migita, C.T., Togashi, S., Minakawa, M., Zhang, X., Yoshida, T. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  6. Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis. Properties of the heme complex of recombinant active enzyme. Migita, C.T., Zhang, X., Yoshida, T. Eur. J. Biochem. (2003) [Pubmed]
  7. Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase. Properties of the heme and enzyme complex. Zhang, X., Migita, C.T., Sato, M., Sasahara, M., Yoshida, T. FEBS J. (2005) [Pubmed]
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