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Gene Review

ARO1  -  pentafunctional protein ARO1p

Saccharomyces cerevisiae S288c

Synonyms: AROM, Pentafunctional AROM polypeptide, YD9302.02, YDR127W
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Disease relevance of ARO1

  • Functional regions within the polypeptide chain have been identified by comparison with the sequences of the five monofunctional Escherichia coli enzymes whose activities correspond with those of the arom multifunctional enzyme [1].

High impact information on ARO1

  • A double-stranded RNA element from a hypovirulent strain of Rhizoctonia solani occurs in DNA form and is genetically related to the pentafunctional AROM protein of the shikimate pathway [2].
  • HPR1 is a gene that is in single copy on chromosome IV of Saccharomyces cerevisiae, closely linked to ARO1, and it codes for a putative protein of 752 amino acids (molecular mass, 88 kilodaltons) [3].
  • Isolation of the ARO1 cluster gene of Saccharomyces cerevisiae [4].
  • The fluorescence emission spectra of both domains had the signal from the tryptophan residues almost completely quenched, giving a tyrosine-dominated spectrum for both the AROM- and QUTR-derived domains [5].
  • The mutant sac6 gene was cloned on the basis of dominant suppression from an act1-1 sac6 mutant library, and was then mapped to chromosome IV, less than 2 cM from ARO1 [6].

Biological context of ARO1


Anatomical context of ARO1

  • Glyphosate-adapted wild-type cells and glyphosate-tolerant cells of a plastid-free mutant of E. gracilis, W10BSmL, were used for organelle isolation and protein extraction, as these cell lines overproduce EPSP synthase and the arom protein, respectively [8].

Associations of ARO1 with chemical compounds

  • The two enzyme forms are inversely regulated at the protein and mRNA levels during light-induced chloroplast development, as demonstrated by the determination of their enzyme activities after non-denaturing polyacrylamide gel electrophoresis and Northern hybridization analysis with a Saccharomyces cerevisiae ARO1 gene probe [8].
  • The molecular basis of glyphosate tolerance is the selective ca. ten-fold overproduction of the multifunctional arom protein catalyzing steps 2-6 in the pre-chorismate pathway [9].
  • The DNA sequences of a portion of the 5-enolpyruvyl shikimate phosphate synthase domain of the arom gene, encoding the pentafunctional AROM protein, were determined from isolates of Pneumocystis carinii from five mammalian host species (rat, human, ferret, rabbit and mouse) [10].
  • The QUTB sequence shows significant homology with the shikimate dehydrogenase function of the complex AROM locus of Aspergillus nidulans, and with the QA-3 quinate dehydrogenase and QA-1S (repressor) genes of Neurospora crassa [11].

Other interactions of ARO1

  • Mutations in ARO1 and ARO2 genes coding for enzymes involved in the common part of the aromatic amino acid pathway completely block the sporulation of Saccharomyces cerevisiae when in a homozygous state, whereas mutations in all the other genes of the same pathway do not [7].
  • Substantial elevation of the levels of the arom protein (25-fold) was achieved in yeast using a vector that exploited the ubiquitin-fusion cleavage system of yeast [12].

Analytical, diagnostic and therapeutic context of ARO1

  • Northern blot analysis and sequence studies indicate that ARO1 is regulated by the well characterised S. cerevisiae 'general control' mechanism [13].
  • The purified material consisted mainly of a polypeptide that co-migrated in SDS-PAGE with intact arom proteins from other species [12].


  1. The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Duncan, K., Edwards, R.M., Coggins, J.R. Biochem. J. (1987) [Pubmed]
  2. A double-stranded RNA element from a hypovirulent strain of Rhizoctonia solani occurs in DNA form and is genetically related to the pentafunctional AROM protein of the shikimate pathway. Lakshman, D.K., Jian, J., Tavantzis, S.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. HPR1, a novel yeast gene that prevents intrachromosomal excision recombination, shows carboxy-terminal homology to the Saccharomyces cerevisiae TOP1 gene. Aguilera, A., Klein, H.L. Mol. Cell. Biol. (1990) [Pubmed]
  4. Isolation of the ARO1 cluster gene of Saccharomyces cerevisiae. Larimer, F.W., Morse, C.C., Beck, A.K., Cole, K.W., Gaertner, F.H. Mol. Cell. Biol. (1983) [Pubmed]
  5. Comparative analysis of the QUTR transcription repressor protein and the three C-terminal domains of the pentafunctional AROM enzyme. Lamb, H.K., Moore, J.D., Lakey, J.H., Levett, L.J., Wheeler, K.A., Lago, H., Coggins, J.R., Hawkins, A.R. Biochem. J. (1996) [Pubmed]
  6. Dominant suppressors of yeast actin mutations that are reciprocally suppressed. Adams, A.E., Botstein, D. Genetics (1989) [Pubmed]
  7. Effect of mutation in the aromatic amino acid pathway on sporulation of Saccharomyces cerevisiae. Lucchini, G., Biraghi, A., Carbone, M.L., de Scrilli, A., Magni, G.E. J. Bacteriol. (1978) [Pubmed]
  8. Cytosolic and plastid forms of 5-enolpyruvylshikimate-3-phosphate synthase in Euglena gracilis are differentially expressed during light-induced chloroplast development. Reinbothe, C., Ortel, B., Parthier, B., Reinbothe, S. Mol. Gen. Genet. (1994) [Pubmed]
  9. Overproduction by gene amplification of the multifunctional arom protein confers glyphosate tolerance to a plastid-free mutant of Euglena gracilis. Reinbothe, S., Ortel, B., Parthier, B. Mol. Gen. Genet. (1993) [Pubmed]
  10. Analysis of genetic diversity at the arom locus in isolates of Pneumocystis carinii. Banerji, S., Lugli, E.B., Miller, R.F., Wakefield, A.E. J. Eukaryot. Microbiol. (1995) [Pubmed]
  11. Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans. Hawkins, A.R., Lamb, H.K., Smith, M., Keyte, J.W., Roberts, C.F. Mol. Gen. Genet. (1988) [Pubmed]
  12. Over-expression of the yeast multifunctional arom protein. Graham, L.D., Gillies, F.M., Coggins, J.R. Biochim. Biophys. Acta (1993) [Pubmed]
  13. The Saccharomyces cerevisiae ARO1 gene. An example of the co-ordinate regulation of five enzymes on a single biosynthetic pathway. Duncan, K., Edwards, R.M., Coggins, J.R. FEBS Lett. (1988) [Pubmed]
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