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Gene Review

phoA  -  bacterial alkaline phosphatase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0378, JW0374, psiA
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Disease relevance of phoA


High impact information on phoA


Chemical compound and disease context of phoA

  • Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions [7].
  • This rapid efficient supercoiling is observed during transcription of membrane-associated gene products, encoded by tet (the gene for tetracycline resistance) and phoA (the gene for E. coli alkaline phosphatase), when the genes are oppositely oriented [8].
  • The rat liver alpha subunit, from arginine 15 to the C-terminal proline 510, has been overexpressed in Escherichia coli using the alkaline phosphatase promoter (phoA) and leader peptide to direct the export of the expressed protein to the bacterial periplasm [9].
  • Amber suppressor mutagenesis, used to create mutant proteins, included: (i) introduction of amber mutations into respective positions of the phoA gene; and (ii) expression of each mutant phoA allele in E. coli strains producing amber suppressor tRNAs specific to Ala, Cys, Gln, Glu, Gly, His, Leu, Lys, Phe, Pro, Ser and Tyr [10].
  • Approximately 90% of the cGSTM1-1 or rGSTT1-1 overexpressed in E. coli under the control of a phoA promoter retained the initiator methionine residue that was absent from the mature isoenzymes isolated from tissues [11].

Biological context of phoA


Anatomical context of phoA

  • Indeed, the pattern of variation observed in BAP-variable phoR strains is phenotypically analogous to phase variation of the H1/H2 flagellum antigen type in Salmonella typhimurium and the molecular switch between the immune and sensitive states in bacteriophage lambda [16].
  • Induction of the phoA promoter of pho regulon and secretion of the product to the periplasm may depress heat shock-like responses and subsequent hydrolysis of the product by cytoplasmic protease [17].
  • Genetic systems for transposon mutagenesis of the L. pneumophila genome (Tn5, Tn903dIIlacZ, MudphoA), including Tn phoA shuttle mutagenesis, have been established and specifically adapted to identify mutants which displayed an impaired capability to multiply inside macrophages and with a reduced in vivo virulence [18].
  • One mutant selected for its impaired ability to invade epithelial cells had an insertion of a Tn phoA transposon within the nlpI gene encoding the lipoprotein NlpI [19].
  • By analyzing reciprocal fusions between crdS and the reporter genes, lacZ and phoA, and assessing the sensitivity of CrdS in spheroplasts to proteinase K, CrdS was shown to be an integral membrane protein with seven transmembrane helices and an Nout-Cin disposition [20].

Associations of phoA with chemical compounds

  • The switching is regulated by the phoM operon and the presence of glucose; the pho-510 mutant form of the phoM operon abolishes both BAP clonal variation and the effect of glucose (B.L. Wanner, J. Bacteriol. 169:900-903, 1987) [21].
  • Induction of malF-phoA fusion proteins, which have no significant effects on membrane integrity, did not alter susceptibility to streptomycin [22].
  • Herein, the phoA promoter without its associated signal peptide is used to regulate expression of the HPRT of Schistosoma mansoni and the ornithine decarboxylase (ODC; L-ornithine carboxy-lyase, EC of Trypanosoma brucei, two enzymes that have been identified as potential targets for antiparasitic chemotherapy [23].
  • Several mtlA-phoA gene fusions encoding fused proteins with N-terminal regions derived from the mannitol permease and C-terminal regions derived from the mature portion of alkaline phosphatase were constructed [24].
  • The amount of initiator methionine was decreased to 40% of the expressed cGSTM1-1 when the isoenzyme was co-expressed with an exogenous methionine aminopeptidase gene under the control of a separate phoA promoter [11].

Physical interactions of phoA

  • It is negatively controlled by phoR as well as by the phosphate-specific transport (PST) system in Escherichia coli. phoA induction is positively controlled by the phoB, M, and R products; it is unaffected by the cAMP and CAP system [25].

Regulatory relationships of phoA

  • However, only phoU mutants express both phoA and psiE constitutively [2].
  • The alteration of DNA sequence was identified for a promoter mutation that results in the expression of phoA independent of the positive control gene phoB and in insensitivity to high phosphate [26].
  • From these results we conclude that the expression of the phoA gene is not always co-regulated with expression of the phoS gene product [27].

Other interactions of phoA

  • Osmo-inducible fusions of phoA were found to ompC and to a gene that is probably proU [28].
  • This phenotype is clearly different from that of the previously isolated class of envZ mutants that exhibit an OmpF- OmpC+ phenotype and a pleiotropic decrease in the expression of several exported protein genes, including lamB and phoA [29].
  • The alternation acted at the level of phoA transcription; it was also recA independent [30].
  • The addition of the local anesthetic procaine to wild-type strains also causes a pleiotropic decrease in the expression of genes ompF, lamB, and phoA [29].
  • Fusions between fhuA and phoA genes were constructed [31].

Analytical, diagnostic and therapeutic context of phoA


  1. The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Kikuchi, Y., Yoda, K., Yamasaki, M., Tamura, G. Nucleic Acids Res. (1981) [Pubmed]
  2. Novel regulatory mutants of the phosphate regulon in Escherichia coli K-12. Wanner, B.L. J. Mol. Biol. (1986) [Pubmed]
  3. Escherichia coli K12 relA strains as safe hosts for expression of recombinant DNA. Schweder, T., Hofmann, K., Hecker, M. Appl. Microbiol. Biotechnol. (1995) [Pubmed]
  4. Modification of the active site of alkaline phosphatase by site-directed mutagenesis. Ghosh, S.S., Bock, S.C., Rokita, S.E., Kaiser, E.T. Science (1986) [Pubmed]
  5. Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation. Udo, H., Munoz-Dorado, J., Inouye, M., Inouye, S. Genes Dev. (1995) [Pubmed]
  6. A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase. Yang, K., Metcalf, W.W. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  7. Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions. Sugiyama, J.E., Mahmoodian, S., Jacobson, G.R. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  8. Dynamics of DNA supercoiling by transcription in Escherichia coli. Cook, D.N., Ma, D., Pon, N.G., Hearst, J.E. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. Mitochondrial ATP synthase. cDNA cloning, amino acid sequence, overexpression, and properties of the rat liver alpha subunit. Lee, J.H., Garboczi, D.N., Thomas, P.J., Pedersen, P.L. J. Biol. Chem. (1990) [Pubmed]
  10. Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. Karamyshev, A.L., Karamysheva, Z.N., Kajava, A.V., Ksenzenko, V.N., Nesmeyanova, M.A. J. Mol. Biol. (1998) [Pubmed]
  11. Co-expression of glutathione S-transferase with methionine aminopeptidase: a system of producing enriched N-terminal processed proteins in Escherichia coli. Hwang, D.D., Liu, L.F., Kuan, I.C., Lin, L.Y., Tam, T.C., Tam, M.F. Biochem. J. (1999) [Pubmed]
  12. A gene fusion approach to the study of pullulanase export and secretion in Escherichia coli. d'Enfert, C., Pugsley, A.P. Mol. Microbiol. (1987) [Pubmed]
  13. Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12. Overbeeke, N., Bergmans, H., van Mansfeld, F., Lugtenberg, B. J. Mol. Biol. (1983) [Pubmed]
  14. Osmotic induction of gene osmC expression in Escherichia coli K12. Gutierrez, C., Devedjian, J.C. J. Mol. Biol. (1991) [Pubmed]
  15. Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12. Makino, K., Shinagawa, H., Amemura, M., Nakata, A. J. Mol. Biol. (1986) [Pubmed]
  16. Bacterial alkaline phosphatase clonal variation in some Escherichia coli K-12 phoR mutant strains. Wanner, B.L. J. Bacteriol. (1986) [Pubmed]
  17. Biosynthesis of a protein containing a nonprotein amino acid by Escherichia coli: L-2-aminohexanoic acid at position 21 in human epidermal growth factor. Koide, H., Yokoyama, S., Kawai, G., Ha, J.M., Oka, T., Kawai, S., Miyake, T., Fuwa, T., Miyazawa, T. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  18. Genetic approaches to study Legionella pneumophila pathogenicity. Ott, M. FEMS Microbiol. Rev. (1994) [Pubmed]
  19. Involvement of lipoprotein NlpI in the virulence of adherent invasive Escherichia coli strain LF82 isolated from a patient with Crohn's disease. Barnich, N., Bringer, M.A., Claret, L., Darfeuille-Michaud, A. Infect. Immun. (2004) [Pubmed]
  20. Topological characterization of an inner membrane (1-->3)-beta-D-glucan (curdlan) synthase from Agrobacterium sp. strain ATCC31749. Karnezis, T., Epa, V.C., Stone, B.A., Stanisich, V.A. Glycobiology (2003) [Pubmed]
  21. Control of bacterial alkaline phosphatase synthesis and variation in an Escherichia coli K-12 phoR mutant by adenyl cyclase, the cyclic AMP receptor protein, and the phoM operon. Wanner, B.L., Wilmes, M.R., Young, D.C. J. Bacteriol. (1988) [Pubmed]
  22. Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin. Wyka, M.A., St John, A.C. Antimicrob. Agents Chemother. (1990) [Pubmed]
  23. High level expression in Escherichia coli of soluble, enzymatically active schistosomal hypoxanthine/guanine phosphoribosyltransferase and trypanosomal ornithine decarboxylase. Craig, S.P., Yuan, L., Kuntz, D.A., McKerrow, J.H., Wang, C.C. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  24. Insertion of the mannitol permease into the membrane of Escherichia coli. Possible involvement of an N-terminal amphiphilic sequence. Yamada, Y., Chang, Y.Y., Daniels, G.A., Wu, L.F., Tomich, J.M., Yamada, M., Saier, M.H. J. Biol. Chem. (1991) [Pubmed]
  25. Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. Wanner, B.L. J. Mol. Biol. (1983) [Pubmed]
  26. Signal sequence of alkaline phosphatase of Escherichia coli. Inouye, H., Barnes, W., Beckwith, J. J. Bacteriol. (1982) [Pubmed]
  27. Control of the synthesis of alkaline phosphatase and the phosphate-binding protein in Escherichia coli. Willsky, G.R., Malamy, M.H. J. Bacteriol. (1976) [Pubmed]
  28. The use of transposon TnphoA to detect genes for cell envelope proteins subject to a common regulatory stimulus. Analysis of osmotically regulated genes in Escherichia coli. Gutierrez, C., Barondess, J., Manoil, C., Beckwith, J. J. Mol. Biol. (1987) [Pubmed]
  29. Isolation and characterization of chain-terminating nonsense mutations in a porin regulator gene, envZ. Garrett, S., Taylor, R.K., Silhavy, T.J. J. Bacteriol. (1983) [Pubmed]
  30. Molecular cloning of the wild-type phoM operon in Escherichia coli K-12. Wanner, B.L., Wilmes, M.R., Hunter, E. J. Bacteriol. (1988) [Pubmed]
  31. Probing FhuA'-'PhoA fusion proteins for the study of FhuA export into the cell envelope of Escherichia coli K12. Günter, K., Braun, V. Mol. Gen. Genet. (1988) [Pubmed]
  32. Characterization of the carbon starvation-inducible and stationary phase-inducible gene slp encoding an outer membrane lipoprotein in Escherichia coli. Alexander, D.M., St John, A.C. Mol. Microbiol. (1994) [Pubmed]
  33. The molecular evolution of bacterial alkaline phosphatase: correlating variation among enteric bacteria to experimental manipulations of the protein. DuBose, R.F., Hartl, D.L. Mol. Biol. Evol. (1990) [Pubmed]
  34. Cloning and restriction mapping of the alkaline phosphatase structural gene (phoA) of Escherichia coli and generation of deletion mutants in vitro. Inouye, H., Michaelis, S., Wright, A., Beckwith, J. J. Bacteriol. (1981) [Pubmed]
  35. Construction of mono- and bivalent human single-chain Fv fragments against the D antigen in the Rh blood group: multimerization effect on cell agglutination and application to blood typing. Furuta, M., Uchikawa, M., Ueda, Y., Yabe, T., Taima, T., Tsumoto, K., Kojima, S., Juji, T., Kumagai, I. Protein Eng. (1998) [Pubmed]
  36. Multiple epitope tagging of expressed proteins for enhanced detection. Hernan, R., Heuermann, K., Brizzard, B. BioTechniques (2000) [Pubmed]
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