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Gene Review

pstS  -  phosphate ABC transporter periplasmic...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3721, JW3706, R2pho, nmpA, phoR2a, ...
 
 
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Disease relevance of pstS

  • These genetic loci are designated as nmpA (at approximately 82.5 min on the E. coli K-12 genetic map), nmpB (8.6 min), and nmpC (12 min) [1].
  • Homologues of the pstS gene were detected in other marine phycoerythrin-containing Synechococcus strains, but not in freshwater or halotolerant species [2].
  • A Xanthomonas oryzae pv. oryzae gene with sequence similarity to an Escherichia coli phosphate-binding protein gene (phoS) produces a periplasmic protein of apparent M(r) 35,000 when expressed in E. coli [3].
 

High impact information on pstS

  • Both PhoP and its truncated DBD domain were found to bind with high affinity to an upstream region of the pstS and phoRP-phoU promoters close to the -35 sequence of each of these promoters [4].
  • Footprinting of the bidirectional phoRP-phoU promoter region showed a 51 bp protected sequence that encompasses four direct repeat units, two of them with high similarity to the protected sequences in the pstS promoter [4].
  • DNase I protection studies revealed a 29 bp protected stretch in the sense strand of the pstS promoter that includes two 11 bp direct repeat units [4].
  • The binding sites of PhoB, three with the sequence TGTCA and one of TTACA, are identified in the pstS promoter [5].
  • In the regulatory region of the gene, a consensus nucleotide sequence shared by the regulatory regions of the phoA, phoS and phoE genes, which we name the "phosphate box", was found [6].
 

Chemical compound and disease context of pstS

 

Biological context of pstS

  • Two specific transcripts were detected, a 4.7-kb polycistronic mRNA spanning the whole operon and a quantitatively dominating 1.2-kb mRNA representing the first gene, pstS [8].
  • The complete sequence (including phoS) contains five open reading frames oriented in the same direction, each preceded by a putative ribosome-binding site near the presumed translation initiation codon ATG [9].
  • The DNA fragment containing the phoS gene, a regulatory gene for alkaline phosphatase, has been isolated from Escherichia coli K-12 chromosomal DNA by cutting off the DNA with Hind III restriction enzyme and by cloning the gene with plasmid vector pTP 4 which was constructed in this study [10].
  • This APEC fimbrial gene cluster, which we have termed stg, is a member of a distinct group of related fimbriae that are located in the glmS-pstS intergenic region of certain E. coli and S. enterica strains [11].
  • The downstream sequence of the Rhodobacter pstS contained five genes similar to pstCAB and phoUB, and its upstream sequence contained a putative regulatory sequence that is analogous to the Pho box involved in phosphate-limitation-induced gene expression in Escherichia coli [12].
 

Anatomical context of pstS

 

Associations of pstS with chemical compounds

  • The phoS product lacks sulfur-containing amino acids and is extractable by treatment with polymyxin sulfate [14].
  • Resistance to arsenate, constitutivty for alkaline phosphatase synthesis and loss of the Pi-binding protein occurred pleiotropically by the same phoS- mutation [15].
  • Hyperproduction of PhoS in strains carrying a multicopy plasmid containing phoS led to partial secretion of the protein [16].
  • Using a phoS-based expression/export vector in the presence of PMSF, 2-4 mg of hybrid protein per liter of culture could be obtained [17].
 

Regulatory relationships of pstS

  • From these results we conclude that the expression of the phoA gene is not always co-regulated with expression of the phoS gene product [14].
 

Other interactions of pstS

  • The complete sequence is transcribed counterclockwise, in the order phoS pstC pstA pstB phoU [9].
  • The new proteins produced in strains carrying nmpA, nmpB, or nmpC mutations did not cross-react with antiserum against a mixture of proteins 1a and 1b, or with antiserum against phage-directed protein 2 [1].
  • A phoB deletion mutant was constructed, and we demonstrated that expression of pstS was strictly dependent on the function of the PhoB protein [18].
 

Analytical, diagnostic and therapeutic context of pstS

References

  1. Identification of three genes controlling production of new outer membrane pore proteins in Escherichia coli K-12. Pugsley, A.P., Schnaitman, C.A. J. Bacteriol. (1978) [Pubmed]
  2. The response of the picoplanktonic marine cyanobacterium Synechococcus species WH7803 to phosphate starvation involves a protein homologous to the periplasmic phosphate-binding protein of Escherichia coli. Scanlan, D.J., Mann, N.H., Carr, N.G. Mol. Microbiol. (1993) [Pubmed]
  3. A homolog of an Escherichia coli phosphate-binding protein gene from Xanthomonas oryzae pv. oryzae. Hopkins, C.M., White, F.F., Heaton, L.A., Guikema, J.A., Leach, J.E. DNA Seq. (1995) [Pubmed]
  4. Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: identification of PHO boxes. Sola-Landa, A., Rodríguez-García, A., Franco-Domínguez, E., Martín, J.F. Mol. Microbiol. (2005) [Pubmed]
  5. DNA binding of PhoB and its interaction with RNA polymerase. Makino, K., Amemura, M., Kawamoto, T., Kimura, S., Shinagawa, H., Nakata, A., Suzuki, M. J. Mol. Biol. (1996) [Pubmed]
  6. 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]
  7. New pleiotropic alkaline phosphatase-negative mutants of Escherichia coli K-12. Heyde, M., Portalier, R. J. Bacteriol. (1982) [Pubmed]
  8. Transcription of the pst operon of Clostridium acetobutylicum is dependent on phosphate concentration and pH. Fischer, R.J., Oehmcke, S., Meyer, U., Mix, M., Schwarz, K., Fiedler, T., Bahl, H. J. Bacteriol. (2006) [Pubmed]
  9. Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships. Surin, B.P., Rosenberg, H., Cox, G.B. J. Bacteriol. (1985) [Pubmed]
  10. Isolation of DNA fragment containing phoS gene of Escherichia coli K-12. Iwakura, M., Shimura, Y., Tsuda, K. J. Biochem. (1982) [Pubmed]
  11. Characterization of Stg fimbriae from an avian pathogenic Escherichia coli O78:K80 strain and assessment of their contribution to colonization of the chicken respiratory tract. Lymberopoulos, M.H., Houle, S., Daigle, F., Léveillé, S., Brée, A., Moulin-Schouleur, M., Johnson, J.R., Dozois, C.M. J. Bacteriol. (2006) [Pubmed]
  12. An abundant periplasmic protein of the denitrifying phototroph Rhodobacter sphaeroides f. sp. denitrificans is PstS, a component of an ABC phosphate transport system. Matsuzaki, M., Abe, M., Hara, S., Iwasaki, Y., Yamamoto, I., Satoh, T. Plant Cell Physiol. (2003) [Pubmed]
  13. Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli. Magota, K., Otsuji, N., Miki, T., Horiuchi, T., Tsunasawa, S., Kondo, J., Sakiyama, F., Amemura, M., Morita, T., Shinagawa, H. J. Bacteriol. (1984) [Pubmed]
  14. 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]
  15. Arsenate-resistant alkaline phosphatase-constitutive mutants of Escherichia coli. Yagil, E., Be'eri, H. Mol. Gen. Genet. (1977) [Pubmed]
  16. Conditions leading to secretion of a normally periplasmic protein in Escherichia coli. Pages, J.M., Anba, J., Lazdunski, C. J. Bacteriol. (1987) [Pubmed]
  17. Improving the stability of a foreign protein in the periplasmic space of Escherichia coli. Anba, J., Bernadac, A., Lazdunski, C., Pagès, J.M. Biochimie (1988) [Pubmed]
  18. Regulation of the phosphate regulon of Escherichia coli: characterization of the promoter of the pstS gene. Kimura, S., Makino, K., Shinagawa, H., Amemura, M., Nakata, A. Mol. Gen. Genet. (1989) [Pubmed]
  19. Complementation tests between alkaline phosphatase-constitutive mutants (phoS and phoT) of Escherichia coli. Levitz, R., Bittan, R., Yagil, E. J. Bacteriol. (1981) [Pubmed]
  20. Chemical heterogeneity of major outer membrane pore proteins of Escherichia coli. Lee, D.R., Schnaitman, C.A., Pugsley, A.P. J. Bacteriol. (1979) [Pubmed]
 
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