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HEM4  -  uroporphyrinogen-III synthase HEM4

Saccharomyces cerevisiae S288c

Synonyms: O5463, ORF1, UROIIIS, UROS, Uroporphyrinogen-III cosynthase, ...
 
 
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Disease relevance of HEM4

  • ORF2, which is expressed only as a 180-kDa fusion protein with ORF1, encodes a single-stranded RNA-binding domain and has the consensus sequence for RNA-dependent RNA polymerases of (+)-strand and double-stranded RNA viruses (pol) [1].
  • The sequence of the carboxyl-terminal hydrophobic region is homologous to an unidentified protein encoded by a reading frame (ORF1) located in one of the cytochrome oxidase operons of Paracoccus denitrificans [2].
  • The hypothetical product of the ACR3 gene shows high similarity to the hypothetical membrane protein encoded by Bacillus subtilis ORF1 of the skin element and weak similarity to the ArsB membrane protein of the Staphylococcus aureus arsenical-resistance operon [3].
 

High impact information on HEM4

  • These mutations are leaky versions of HEM2 and HEM4, respectively; addition of exogenous hemin reverses the suppressing effects of slu1 and slu2 [4].
  • The sequence of L-A cDNA clones revealed two open reading frames (ORF), ORF1 and ORF2 [5].
  • Although the major coat protein of the viral particles is encoded by ORF1, the 180-kDa protein is derived from the entire double-stranded RNA genome by fusing ORF1 and ORF2, probably by a -1 translational frameshift [5].
  • Cell extracts of a hem4 mutant incubated with delta-aminolevulinate accumulated coproporphyrin III suggesting a block in coproporphyrinogenase, the enzyme which converts coproporphyrinogen III to protoporphyrinogen [6].
  • Since hem4 and hem5 mutants have sulfite reductase activity under all growth conditions, they are blocked after uroporphyrin III [6].
 

Biological context of HEM4

  • A hem4 delta disruption mutation was constructed which had phenotypes identical to the cyt mutation [7].
  • It contains two open reading frames, ORF1 and ORF2, consisting of 723 and 417 base pairs, respectively [8].
  • By selective deletion of either reading frame it was shown that only ORF1 containes the information necessary to complement the ts2326 mutation [8].
  • As for the latter, ORF1 existing on the two other plasmids is lacking on pPac1-1 [9].
  • A programmed +1 ribosomal frameshift occurs at the last codon of ORF1 and results in the production of full-length antizyme protein [10].
 

Anatomical context of HEM4

  • We have shown previously that the N-terminal part of ORF1 contains the information leading to vesiculation of mitochondria and that the 36-kDa protein localizes to mitochondria [11].
 

Associations of HEM4 with chemical compounds

  • The final common biosynthetic step in tetrapyrrole biosynthesis is the generation of uroporphyrinogen by uroporphyrinogen III synthase, whereby the D ring of hydroxymethylbilane is flipped during ring closure to generate the asymmetrical structure of uroporphyrinogen III [12].

References

  1. A -1 ribosomal frameshift in a double-stranded RNA virus of yeast forms a gag-pol fusion protein. Dinman, J.D., Icho, T., Wickner, R.B. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase. Nobrega, M.P., Nobrega, F.G., Tzagoloff, A. J. Biol. Chem. (1990) [Pubmed]
  3. Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Bobrowicz, P., Wysocki, R., Owsianik, G., Goffeau, A., Ułaszewski, S. Yeast (1997) [Pubmed]
  4. A yeast sterol auxotroph (erg25) is rescued by addition of azole antifungals and reduced levels of heme. Gachotte, D., Pierson, C.A., Lees, N.D., Barbuch, R., Koegel, C., Bard, M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames. Icho, T., Wickner, R.B. J. Biol. Chem. (1989) [Pubmed]
  6. Yeast mutants deficient in heme biosynthesis and a heme mutant additionally blocked in cyclization of 2,3-oxidosqualene. Gollub, E.G., Liu, K.P., Dayan, J., Adlersberg, M., Sprinson, D.B. J. Biol. Chem. (1977) [Pubmed]
  7. Isolation of the gene HEM4 encoding uroporphyrinogen III synthase in Saccharomyces cerevisiae. Amillet, J.M., Labbe-Bois, R. Yeast (1995) [Pubmed]
  8. Isolation of a nuclear yeast gene involved in the mitochondrial import of cytoplasmically synthesized precursor proteins. Langgut, W., Entrup, R., Schweizer, E. Curr. Genet. (1986) [Pubmed]
  9. Autonomous cytoplasmic linear plasmid pPac1-1 of Pichia acaciae: molecular structure and expression studies. Jeske, S., Meinhardt, F. Yeast (2006) [Pubmed]
  10. Polyamine sensing during antizyme mRNA programmed frameshifting. Petros, L.M., Howard, M.T., Gesteland, R.F., Atkins, J.F. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Mitochondrial targeting and membrane anchoring of a viral replicase in plant and yeast cells. Weber-Lotfi, F., Dietrich, A., Russo, M., Rubino, L. J. Virol. (2002) [Pubmed]
  12. Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase. Schubert, H.L., Raux, E., Matthews, M.A., Phillips, J.D., Wilson, K.S., Hill, C.P., Warren, M.J. Biochem. Soc. Trans. (2002) [Pubmed]
 
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