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Chapter 12 : Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate

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Abstract:

This chapter focuses on the control of the Pho regulon by the signal transduction pathways involving the P sensor PhoR, the catabolite regulatory sensor CreC, and acetyl phosphate. It is also poorly understood whether cross regulation by CreC or by acetyl phosphate has a bonafide role in Pho regulon control under certain conditions in normal cells. Therefore, some speculations are provided about the nature of the P signal transduction pathway and about the roles of CreC and acetyl phosphate in Pho regulon control. The chapter discusses signal transduction pathways of the Pho regulon. A P repression complex may contain all components of the Pst system, PhoU, and PhoR, because all these are required for P repression. By testing effects due to and mutations, it was shown that activation of the Pho regulon in the absence of both PhoR and CreC requires acetyl phosphate synthesis. Evolutionarily related proteins share sequence similarities at the protein level with other members of the same family. Therefore, sensors are probably structurally and functionally similar to other sensors, and response regulators are probably structurally and functionally similar to other response regulators. The primary control of the Pho regulon involves a signal transduction pathway responsive to the extracellular P level.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12

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Bacterial Proteins
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Figures

Image of FIGURE 1
FIGURE 1

Alternative repression complexes for signal transduction by Plimitation. P control may involve P binding only to PstS or to both PstS and a regulatory site, which may be on a different Pst component or on PhoR. A hypothetical regulatory site is indicated by a question mark in parentheses. In repression complex I, the PhoR repressor form is shown as a monomer, which is intended to imply any lower oligomeric form. In repression complex II, the PhoR repressor form is shown as a dimer, which is intended to imply any higher oligomeric form. These complexes are compatible with alternative mechanisms for inter-conversion of the PhoR repressor and activator forms as described in the text.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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Image of FIGURE 2
FIGURE 2

Mechanisms of detection of environmental P.The stoichiometric and regulatory site mechanisms are illustrated. In accordance with either mechanism, the PhoR repressor form may be associated with a repression complex when P is in excess. The stoichiometric mechanism may lead to the release of PhoR from those complexes to which no P is bound under conditions of Pi limitation. The regulatory site mechanism may lead to a conformational change in PhoR (without its release from a repression complex) due to absence of P occupancy of the regulatory site. PhoR is shown as a monomer solely for the purpose of illustration. No particular oligomeric form of PhoR is implied.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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Image of FIGURE 3
FIGURE 3

Mechanisms for interconversion of PhoR and PhoR by environmental P. Association-dissociation and conformational change mechanisms are illustrated. PhoRR may prevail when the environmental P level is in excess (an environmental Pi level greater than about 4 µM); and PhoR may prevail under conditions of P limitation (an environmental Pi level less than about 4 µM). PhoR may be a phospho-PhoB (PhoB-P) phosphatase, and PhoR is a phosphoryl transferase and PhoB kinase. Accordingly, PhoRA may autophosphorylate on a histidine residue and transfer this phosphoryl group to an aspartate residue on PhoB. Although PhoR and PhoR are depicted in association with PhoB and PhoB-P, respectively, these associations are likely to be transient. No particular oligomeric form of PhoR is implied, except that PhoRA is probably a dimer or higher oligomer. This is because the mechanism of auto-phosphorylation for the PhoR homologs EnvZ and CheA involves phosphorylation of one subunit by the other subunit ( ). The oligomeric structure(s) of PhoR is unknown.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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Image of FIGURE 4
FIGURE 4

Pta-AckA pathway for ATP synthesis.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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Image of FIGURE 5
FIGURE 5

Pathways for Pi incorporation into ATP. AtpIBEFHAGDC, ATP synthase; Gap, glyceraldehyde-3-phosphate dehydrogenase; Pgk, phosphoglycerate kinase; PMF, proton motive force; SucCD, succinyl coenzyme A synthetase.

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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Image of FIGURE 6
FIGURE 6

Multiple controls of PhoB phosphorylation by PhoR, CreC, and acetyl phosphate. A signal for the extracellular (ext) Plevel controls the Pho regulon via the Pst system, PhoU, and the Pi sensor PhoR. A signal for an unknown catabolite (which may be an intermediate of a central pathway of carbon, energy, and P metabolism) controls the Pho regulon via a central pathway and the catabolite sensor CreC. A signal for ATP synthesis controls the Pho regulon via the Pta-AckA pathway and acetyl phosphate. PhoR, CreC, and acetyl phosphate, in turn, activate the regulator PhoB by phosphorylation. PhoB has been shown to be directly phosphorylated by acetyl phosphate in vitro (Hiratsu et al., personal communication). Nevertheless, it has not been established whether acetyl phosphate acts directly on PhoB as a phosphoryl donor or indirectly via an unknown sensor in vivo ( ). The solid arrow symbolizes signal transduction by P limitation. The dashed arrows symbolize signal transduction due to (proposed) cross regulation. Adapted from .

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
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References

/content/book/10.1128/9781555818319.chap12
1. Adams, M. D.,, and D. L. Oxender. 1989. Bacterial periplasmic binding protein tertiary structures. J. Biol. Chem. 264:1573915742.
2. Amemura, M.,, K. Makino,, H. Shinagawa,, A. Kobayashi,, and A. Nakata. 1985. Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli. J. Mol. Biol. 184:241250.
3. Amemura, M.,, K. Makino,, H. Shinagawa,, and A. Nakata. 1986. Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon. J. Bacteriol. 168:294302.
4. Amemura, M.,, K. Makino,, H. Shinagawa,, and A. Nakata. 1990. Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2. J. Bacteriol. 172:63006307.
5. Ames, G. F.-L. 1986a. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 55:397125.
6. Ames, G. F.-L. 1986b. The basis of multidrug resistance in mammalian cells: homology with bacterial transport. Cell 47:323324.
7. Baichwal, V.,, D. Liu,, and G. F. - L. Ames. 1993.The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proc. Natl. Acad. Sci. USA 90:620624.
8. Chang, B.,, and B. L. Wanner. Unpublished data.
9. Chang, C. N.,, W.-J. Kuang,, and E. Y. Chen. 1986. Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene 44:121125.
10. Chen, C.-J.,, J. E. Chin,, K. Ueda,, D. P. Clark,, I. Pastan,, M. M. Gottesman,, and I. B. Roninson. 1986. Internal duplication and homology with bacterial transport proteins in the mdri (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47:381389.
11. Chen, C.-M.,, Q. Ye,, Z. Zhu,, B. L. wanner,, and C. T. Walsh. 1990. Molecular biology of carbonphosphorus bond cleavage: cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coliB. J. Biol. Chem. 265:44614471.
12. Cox, G. Personal communication.
13. Cox, G. B.,, H. Rosenberg,, J. A. Downie,, and S. Silver. 1981. Genetic analysis of mutants affected in the Pst inorganic phosphate transport system. J. Bacteriol. 148:19.
14. Cox, G. B.,, D. Webb,, J. Godovac-Zimmermann,, and H. Rosenberg. 1988. Arg-220 of the PstA protein is required for phosphate transport through the phosphate-specific transport system in Escherichia coli but not for alkaline phosphatase repression. J. Bacteriol. 170:22832286.
15. Cox, G. B.,, D. Webb,, and H. Rosenberg. 1989. Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli Pst system. J. Bacteriol. 171: 15311534.
16. Davis, E. O.,, and P. J. F. Henderson. 1987. The cloning and DNA sequence of the gene xylE for xylose-proton symport in Escherichia coli K12. J. Biol. Chem. 262:1392813932.
17. Davis, E. O.,, and P. J. F. Henderson. 1987. The cloning and DNA sequence of the gene xylE for xylose-proton symport in Escherichia coli K12. J. Biol. Chem. 262:1392813932.
18. Foote, S. J.,, D. E. Kyle,, R. K. Martin,, A. M. J. Oduola,, K. Forsyth,, D. J. Kemp,, and A. F. Cowman. 1990. Several alleles of the multidrug-resistance gene are closely linked to chloroquine resistance in Plasmodium falciparum. Nature (London) 345:255258.
19. Forst, S.,, D. Comeau,, S. Norioka,, and M. Inouye. 1987. Localization and membrane topology of EnvZ, a protein involved in osmoregulation of OmpF and OmpC in Escherichia coli. J. Biol. Chem. 262:1643316438.
20. Gegner, J. A.,, D. R. Graham,, A. F. Roth,, and F. W. Dahlquist. 1992. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 70:975982.
21. Gros, P.,, J. Croop,, and D. Housman. 1986. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47:371380.
22. Hazelbauer, G. L. 1992. Bacterial chemoreceptors. Curr. Opin. Struct. Biol. 2:505510.
23. Hiratsu, K.,, K. Makino,, A. Nakata,, and H. Shinagawa. Personal communication.
24. Hoch, J. A. 1993. Regulation of the phosphorelay and the initiation of sporulation in Bacillus subtilis. Annu. Rev. Microbiol. 47:441465.
25. Hyde, S. C.,, P. Emsley,, M. J. Hartshorn,, M. M. Mimmack,, U. Gileadi,, S. R. Pearce,, M. P. Gallagher,, D. R. Gill,, R. E. Hubbard,, and C. F. Higgins. 1990. Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature (London) 346:362365.
26. Igo, M. M.,, A. J. Ninfa,, and T. J. Silhavy. 1989. A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation. Genes Dev. 3:598605.
27. Igo, M. M.,, A. J. Ninfa,, and T. J. Silhavy. 1989. A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation. Genes Dev. 3:598605.
28. Jones, T. C. 1969. Genetic control of basal level of alkaline phosphatase in Escherichia coli. Mol. Gen. Genet. 105:91100.
29. Kaplan, H. Personal communication.
30. Kaplan, H. B.,, A. Kuspa,, and D. Kaiser. 1991. Suppressors that permit A-signal-independent developmental gene expression in Myxococcus xanthus. J. Bacteriol. 173:14601470.
31. Kasahara, M.,, K. Makino,, M. Amemura,, and A. Nakata. 1989. Nucleotide sequence of the ugpQ gene encoding glycerophosphoryl diester phosphodiesterase of Escherichia coli K12. Nucleic Acids Res. 17:2854.
32. Kasahara, M.,, K. Makino,, M. Amemura,, A. Nakata,, and H. Shinagawa. 1991. Dual regulation of the ugp operon by phosphate and carbon starvation at two interspaced promoters. J. Bacteriol. 173:549558.
33. Kim, S.-K.,, K. Makino,, M. Amemura,, H. Shinagawa,, and A. Nakata. 1993. Molecular analysis of the phoH gene, belonging to the phosphate regulon in Escherichia coli. J. Bacteriol. 175:13161324.
34. Kofoid, E. C.,, and J. S. Parkinson. 1988. Transmitter and receiver modules in bacterial signaling proteins. Proc. Natl. Acad. Sci. USA 85:49814985.
35. Lee, K.-S.,, W. W. Metcalf,, and B. L. Wanner. 1992. Evidence for two phosphonate degradative pathways in Enterobacter aerogenes. J. Bacteriol. 174:25012510.
36. Luecke, H.,, and E. A. Quiocho. 1990. High specificity of a phosphate transport protein determined by hydrogen bonds. Nature (London) 347:402406.
37. Magasanik, B. 1993. The regulation of nitrogen utilization in enteric bacteria. J. Cell. Biochem. 51:3440.
38. Magota, K.,, N. Otsuji,, T. Miki,, T. Horiuchi,, S. Tsunasawa,, J. Kondo,, E. Sakiyama,, M. Amemura,, T. Morita,, H. Shinagawa,, and A. Nakata. 1984. Nucleotide sequence of the phoS gene, the structural gene for the phosphate-binding protein of Escherichia coli. J. Bacteriol. 157:909917.
39. Makino, K.,, M. Amemura,, S.-K. Kim,, A. Nakata,, and H. Shinagawa. 1993. Role of the σ70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Genes Dev. 7:149160.
40. Makino, K.,, M. Amemura,, S.-K. Kim,, H. Shinagawa,, and A. Nakata,. 1992. Signal transduction of the phosphate regulon in Escherichia coli mediated by phosphorylation, p. 191200. In S. Papa,, A. Azzi,, and J. M. Tager (ed.), Adenine Nucleotides in Cellular Energy Transfer and Signal Transduction. Birkhaeuser Verlag, Basel, Switzerland.
41. Makino, K.,, S.-K. Kim,, H. Shinagawa,, M. Amemura,, and A. Nakata. 1991. Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12. J. Bacteriol. 173:26652672.
42. Makino, K.,, H. Shinagawa,, M. Amemura,, T. Kawamoto,, M. Yamada,, and A. Nakata. 1989. Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J. Mol. Biol. 210:551559.
43. Metcalf, W. W.,, P. M. Steed,, and B. L. Wanner. 1990. Identification of phosphate-starvation-inducible genes in Escherichia coli K-12 by DNA sequence analysis ofpsi::ZocZ(Mu d1) transcriptional fusions. J. Bacteriol. 172:31913200.
44. Metcalf, W. W.,, and B. L. Wanner. 1993. Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation using TnphoA' elements. J. Bacteriol. 175:34303442.
45. Ninfa, A. J.,, E. G. Ninfa,, A. N. Lupas,, A. Stock,, B. Magasanik,, and J. Stock. 1988. Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proc. Natl. Acad. Sci. USA 85:54925496.
46. Nixon, B. T.,, C. W. Ronson,, and E. M. Ausubel. 1986. Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC. Proc. Natl. Acad. Sci. USA 83:78507854.
47. Overbeeke, N.,, H. Bergmans,, E. V. Mansfeld,, and B. Lugtenberg. 1983. Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K 12 J. Mol. Biol. 163:513532.
48. Overduin, P.,, W. Boos,, and J. Tommassen. 1988. Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to the maltose system. Mol. Microbiol. 2:767775.
49. Parkinson, J. S.,, and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71112.
50. Ronson, C. W.,, B. T. Nixon, and E M. Ausubel. 1987. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 49:579581.
51. Scholten, M.,, and J. Tommassen. 1993. Topology of the PhoR protein of Escherichia coli and functional analysis of internal deletion mutants. Mol. Microbiol. 8:269275.
52. Shulman, R. G.,, T. R. Brown,, K. Ugurbil,, S. Ogawa,, S. M. Cohen,, and J. A. den Hollander. 1979. Cellular applications of 31 P and 13 C nuclear magnetic resonance. Science 205:160166.
53. Shuttleworth, H.,, J. Taylor,, and N. Minton. 1986. Sequence of the gene for alkaline phosphatase from Escherichia coli JM83. Nucleic Acids Res. 14:8689.
54. Steed, P. M.,, and B. L. Wanner. 1993. Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon. J. Bacteriol. 175:67976809.
55. Stock, J. B.,, A. J. Ninfa,, and A. M. Stock. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53:450490.
56. Surin, B. P.,, N. E. Dixon,, and H. Rosenberg. 1986. Purification of the PhoU protein, a negative regulator of the Pho regulon of Escherichia coliK-12. J. Bacteriol. 168:631635.
57. Surin, B. P.,, D. A. Jans,, A. L. Fimmel,, D. C. Shaw,, G. B. Cox,, and H. Rosenberg. 1984. Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene. J. Bacteriol. 157:772778.
58. Surin, B. P.,, H. Rosenberg,, and G. B. Cox. 1985. Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships. J. Bacteriol. 161:189198.
59. Swanson, R. V.,, R. B. Bourret,, and M. I. Simon. 1993. Intermolecular complementation of the kinase activity of CheA. Mol. Microbiol. 8:435441.
60. Tommassen, J.,, K. Eiglmeier,, S. T. Cole,, P. Overduin,, T. J. Larson,, and W. Boos. 1991. Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli. Mol. Gen. Genet. 226:321327.
61. Wanner, B. L. 1987a. Control of phoR-dependent bacterial alkaline phosphatase clonal variation by the phoM region. J. Bacteriol. 169:900903.
62. Wanner, B. L., 1987b. Phosphate regulation of gene expression in Escherichia coli, p. 13261333. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 2. American Society for Microbiology, Washington, D.C..
63. Wanner, B. L., 1990. Phosphorus assimilation and its control of gene expression in Escherichia coli, p. 152163. In G. Hauska, and R. Thauer (ed.), The Molecular Basis of Bacterial Metabolism. Springer-Verlag, Heidelberg.
64. Wanner, B. L. 1992. Minireview. Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria? J. Bacteriol. 174:20532058.
65. Wanner, B. L. 1993. Gene regulation by phosphate in enteric bacteria. J. Cell. Biochem. 51:4754.
66. Wanner, B. L., 1994. Multiple controls of the Escherichia coli Pho regulon by the Pi sensor PhoR, the catabolite regulatory sensor CreC, and acetyl phosphate, p. 1321. In A. Torriani-Gorini,, E. Yagil,, and S. Silver (ed.), Phosphate in Microorganisms: Cellular and Molecular Biology. American Society for Microbiology, Washington, D.C..
67. Wanner, B. L.,, and B.-D. Chang. 1987. The phoBR operon in Escherichia coli K-12. J. Bacteriol. 169:55695574.
68. Wanner, B. L.,, and P. Latterell. 1980. Mutants affected in alkaline phosphatase expression: evidence for multiple positive regulators of the phosphate regulon in Escherichia coli. Genetics 96: 242266.
69. Wanner, B. L.,, A. Sarthy,, and J. R. Beckwith. 1979. Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteins. J. Bacteriol. 140:229239.
70. Wanner, B. L.,, M. R. Wilmes,, and D. C. Young. 1988. 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. J. Bacteriol. 170: 10921102.
71. Wanner, B. L.,, and M. R. Wilmes-Riesenberg. 1992. Involvement of phosphotransacetylase, acetate kinase, and acetyl phosphate synthesis in the control of the phosphate regulon in Escherichia coli. J. Bacteriol. 174:21242130.
72. Willsky, G. R.,, R. L. Bennett,, and M. H. Malamy. 1973. Inorganic phosphate transport in Escherichia coli: involvement of two genes which play a role in alkaline phosphatase regulation. J. Bacteriol. 113: 529539.
73. Willsky, G. R.,, and M. H. Malamy. 1976. Control of the synthesis of alkaline phosphatase and the phosphate-binding protein in Escherichia coli. J. Bacteriol. 127:595609.
74. Wilmes-Riesenberg, M. R.,, and B. L. Wanner. 1992. TnphoA and TnphoA' elements for making and switching fusions for study of transcription, translation, and cell surface localization. J. Bacteriol. 174:45584575.
75. Wilmes-Riesenberg, M. R.,, and B. L. Wanner. Unpublished data.
76. Wolfe, A. J.,, and R. C. Stewart. 1993. The short form of the CheA protein restores kinase activity and chemotactic ability to kinase-deficient mutants. Proc. Natl. Acad. Sci. USA 90:15181522.
77. Yang, Y.,, and M. Inouye. 1991. Intermolecular complementation between two defective mutant signal-transducing receptors of Escherichia coli. Proc. Natl. Acad. Sci. USA 88:1105711061.
78. Yang, Y.,, and M. Inouye. 1993. Requirement of both kinase and phosphatase activities of an Escherichia coli receptor (Tazl) for ligand-dependent signal transduction. J. Mol. Biol. 231:335342.

Tables

Generic image for table
TABLE 1

Effects of P limitation and catabolites on Pho regulon control

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
Generic image for table
TABLE 2

Genes involved in P-independent controls of the Pho regulon

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12
Generic image for table
TABLE 3

Pi-regulated genes of the Pho regulonª

Citation: Wanner B. 1995. Signal Transduction and Cross Regulation in the Phosphate Regulon by PhoR, CreC, and Acetyl Phosphate, p 203-221. In Hoch J, Silhavy T (ed), Two-Component Signal Transduction. ASM Press, Washington, DC. doi: 10.1128/9781555818319.ch12

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