Response Regulator Proteins and Their Interactions with Histidine Protein Kinases

Histidine Kinases in Signal Transduction

Volumn , Issue , 2002, Pages 237-271

  Stock, Ann M ^a   West, Ann H ^b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF OKLAHOMA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PHOSPHATASES; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

AUTOPHOSPHORYLATION; EFFECTOR DOMAINS; HISTIDINE PROTEIN KINASE; PHOSPHATASE ACTIVITY; PHOSPHORYL GROUPS; REGULATORY DOMAIN; RESPONSE REGULATORS; TWO-COMPONENT SIGNAL TRANSDUCTION;

PLANTS (BOTANY);

EID: 84902408786     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012372484-7/50013-8     Document Type: Chapter

References (169)

1. Stock J.B., Ninfa A.J., Stock A.M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 1989, 53:450-490.
2. Bourret R.B., Borkovich K.A., Simon M.I. Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu. Rev. Biochem. 1991, 60:401-441.
3. Volz K. Structural conservation in the CheY superfamily. Biochemistry 1993, 32:11741-11753.
4. Stock J.B., Surette M.G., Levit M., Park P. Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis. Two-Component Signal Transduction 1995, 25-51. American Society for Microbiology, Washington, DC. J.A. Hoch, T.J. Silhavy (Eds.).
5. Volz K. Structural and functional conservation in response regulators. Two-Component Signal Transduction 1995, 53-64. American Society for Microbiology Press, Washington, D.C. J.A. Hoch, T.J. Silhavy (Eds.).
6. Mizuno T. Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli. DNA Res. 1997, 4:161-168.
7. Chang C., Stewart R.C. The two-component system. Regulation of diverse signaling pathways in prokaryotes and eukaryotes. Plant Physiol. 1998, 117:723-731.
8. Loomis W.F., Kuspa A., Shaulsky G. Two-component signal transduction systems in eukaryotic microorganisms. Curr. Opin. Microbiol. 1998, 1:643-648.
9. Mizuno T. His-Asp phosphotransfer signal transduction. J. Biochem. 1998, 123:555-563.
10. D'Agostino I.B., Kieber J.J. Phosphorelay signal transduction: The emerging family of plant response regulators. Trends Biochem. Sci. 1999, 24:452-456.
11. Perraud A.-L., Weiss V., Gross R. Signalling pathways in two-component phosphorelay systems. Trends Microbiol. 1999, 7:115-120.
12. Hoch J.A. Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 2000, 3:165-170.
13. Robinson V.L., Buckler D.R., Stock A.M. A tale of two components: A novel kinase and a regulatory switch. Nature Struct. Biol. 2000, 7:628-633.
14. Stock A.M., Robinson V.L., Goudreau P.N. Two-component signal transduction. Annu. Rev. Biochem. 2000, 69:183-215.
15. Stock J., Da Re S. Signal transduction: Response regulators on and off. Curr. Biol. 2000, 10:R420-R424.
16. Lukat G.S., McCleary W.R., Stock A.M., Stock J.B. Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc. Natl. Acad. Sci. USA 1992, 89:718-722.
17. Feng J., Atkinson M.R., McCleary W., Stock J.B., Wanner B.L., Ninfa A.J. Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli. J. Bacteriol. 1992, 174:6061-6070.
18. McCleary W.R., Stock J.B., Ninfa A.J. Is acetyl phosphate a global signal in Escherichia coli?. J. Bacteriol. 1993, 175:2793-2798.
19. McCleary W.R., Stock J.B. Acetyl phosphate and the activation of two-component response regulators. J. Biol. Chem. 1994, 269:31567-31572.
20. Hess J.F., Oosawa K., Kaplan N., Simon M.I. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 1988, 53:79-87.
21. Zapf J., Madhusudan M., Grimshaw C.E., Hoch J.A., Varughese K.I., Whiteley J.M. A source of response regulator autophosphatase activity: The critical role of a residue adjacent to the Spo0F autophosphorylation active site. Biochemistry 1998, 37:7725-7732.
22. Stock A.M., Mottonen J.M., Stock J.B., Schutt C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 1989, 337:745-749.
23. Stock J.B., Stock A.M., Mottonen J.M. Signal transduction in bacteria. Nature 1990, 344:395-400.
24. Volz K., Matsumura P. Crystal structure of Escherichia coli CheY refined at 1.7 resolution. J. Biol. Chem. 1991, 266:15511-15519.
25. Madhusudan, Zapf J., Whiteley J.M., Hoch J.A., Xuong N.H., Varughese K.I. Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis. Structure 1996, 4:679-690.
26. Djordjevic S., Goudreau P.N., Xu Q., Stock A.M., West A.H. Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc. Natl. Acad. Sci. USA 1998, 95:1381-1386.
27. Solà M., Gomis-Rüth F.X., Serrano L., González A., Coll M. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J. Mol. Biol. 1999, 285:675-687.
28. Baikalov I., Schröder I., Kaczor-Grzeskowiak M., Grzeskowiak K., Gunsalus R.P., Dickerson R.E. Structure of the Escherichia coli response regulator NarL. Biochemistry 1996, 35:11053-11061.
29. Volkman B.F., Nohaile M.J., Amy N.K., Kustu S., Wemmer D.E. Three-dimensional solution structure of the N-terminal receiver domain of NtrC. Biochemistry 1995, 34:1413-1424.
30. Lewis R.J., Muchova K., Brannigan J.A., Barak I., Leonard G., Wilkinson A.J. Domain swapping in the sporulation response regulator Spo0A. J. Mol. Biol. 2000, 297:757-770.
31. Gouet P., Fabry B., Guillet V., Birck C., Mourey L., Kahn D., Samama J.-P. Structural transitions in the FixJ receiver domain. Structure 1999, 7:1517-1526.
32. Muller-Dieckmann H.J., Grantz A.A., Kim S.H. The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1. Structure Fold. Des. 2000, 7:1547-1556.
33. Birck C., Liu W., Cabantous S., Hulett M., Samama J.-P. X-ray crystal structure of the receiver domain of PhoP. VI Conference on Bacterial Locomotion and Signal Transduction 2001.
34. Buckler D.R., Stock A.M. Structural analysis of a full-length OmpR homology from Thermotoga maritima. VI Conference on Bacterial Locomotion and Signal Transduction 2001.
35. Sanders D.A., Gillece-Castro B.L., Stock A.M., Burlingame A.L., Koshland D.E. Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J. Biol. Chem. 1989, 264:21770-21778.
36. 1) of Escherichia coli. Proc. Natl. Acad. Sci. USA 1988, 85:8919-8923.
37. Lukat G.S., Stock A.M., Stock J.B. Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis. Biochemistry 1990, 29:5436-5442.
38. Needham J.V., Chen T.Y., Falke J.J. Novel ion specificity of a carboxylate cluster Mg(II) binding site: Strong charge slectivity and weak size selectivity. Biochemistry 1993, 32:3363-3367.
39. 2+-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry 1993, 32:13375-13380.
40. 2+, hydrogen bonding, and steric factors on rate and equilibrium constants for phosphoryl transfer between carboxylate ions and pyridines. J. Am. Chem. Soc. 1990, 112:1942-1950.
41. Lewis R.J., Brannigan J.A., Muchová K., Barák I., Wilkinson A.J. Phosphorylated aspartate in the structure of a response regulator protein. J. Mol. Biol. 1999, 294:9-15.
42. Birck C., Mourey L., Gouet P., Fabry B., Schumacher J., Rousseau P., Kahn D., Samama J.-P. Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure Fold. Des. 1999, 7:1505-1515.
43. Kern D., Volkman B.F., Luginbuhl P., Nohaile M.J., Kustu S., Wemmer D.E. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 1999, 40:894-898.
44. Silversmith R.E., Bourret R.B. Synthesis and characterization of a stable analog of the phosphorylated form of the chemotaxis protein CheY. Protein Engin. 1998, 11:205-212.
45. Halkides C.J., Zhu X., Phillion D.P., Matsumura P., Dahlquist F.W. Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry 1998, 37:13674-13680.
46. Halkides C.J., McEvoy M.M., Casper E., Matsumura P., Volz K., Dahlquist F.W. The 1.9 resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry 2000, 39:5280-5286.
47. Yan D., Cho H.S., Hastings C.A., Igo M.M., Lee S.Y., Pelton J.G., Stewart V., Wemmer D.E., Kustu S. Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators. Proc. Natl. Acad. Sci. USA 1999, 96:14789-14794.
48. Lee S.-Y., Cho H.S., Pelton J.G., Yan D., Henderson R.K., King D.S., Huang L.-S., Kustu S., Berry E.A., Wemmer D.E. Crystal structure of an activated response regulator bound to its target. Nature Struct. Biol. 2001, 8:52-56.
49. Wemmer D. VI Conference on Bacterial Locomotion and Signal Transduction 2001.
50. +. Biochemistry 1994, 33:10470-10476.
51. West A.H., Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 2001, 26.
52. Bellsolell L., Prieto J., Serrano L., Coll M. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J. Mol. Biol. 1994, 238:489-495.
53. Ganguli S., Wang H., Matsumura P., Volz K. Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.1- structure of a threonine to isoleucine mutant at position 87 of CheY. J. Biol. Chem. 1995, 270:1-8.
54. Jiang M., Bourret R.B., Simon M.I., Volz K. Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.3 structure of an aspartate to lysine mutant at position 13 of CheY. J. Biol. Chem. 1997, 272:11850-11855.
55. Zhu X., Rebello J., Matsumura P., Volz K. Crystal structures of CheY mutants Y106W and T87I/Y106W: CheY activation correlates with movement of residue 106. J. Biol. Chem. 1997, 272:5000-5006.
56. Feher V.A., Cavanagh J. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature 1999, 400:289-293.
57. Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntosh L.P., Rance M., Skelton N.J., Dahlquist F.W., Cavanagh J. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: Implications for phosphorylation and molecular recognition. Biochemistry 1997, 36:10015-10025.
58. 15N) NMR spectroscopy. Biochemistry 1994, 33:10731-10742.
59. Nohaile M., Kern D., Wemmer D., Stedman K., Kustu S. Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface. J. Mol. Biol. 1997, 273:299-316.
60. Volkman B.F., Lipson D., Wemmer D.E., Kern D. Two-state allosteric behavior in a single domain signaling protein. Science 2001, 291:2429-2433.
61. Tzeng Y.-L., Hoch J.A. Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis. J. Mol. Biol. 1997, 272:200-212.
62. Tzeng Y.-L., Feher V.A., Cavanagh J., Perego M., Hoch J.A. Characterization of interactions between a two-component response regulator, Spo0F, and its phosphatase, RapB. Biochemistry 1998, 37:16538-16545.
63. Aiba H., Nakasai F., Mizushima S., Mizuno T. Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in a stimulation of its DNA-binding ability. J. Biochem. 1989, 106:5-7.
64. Huang K.-E., Lan C.-Y., Igo M.M. Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR. Proc. Natl. Acad. Sci. USA 1997, 94:2828-2832.
65. Head C.G., Tardy A., Kenney L.J. Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites. J. Mol. Biol. 1998, 281:857-870.
66. Ames S.K., Frankema N., Kenney L.J. C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc. Natl. Acad. Sci. USA 1999, 96:11792-11797.
67. Qin L., Yoshida T., Inouye M. The critical role of DNA in the equilibrium between OmpR and phosphorylated OmpR mediated by EnvZ in Escherichia coli. Proc. Natl. Acad. Sci. USA 2001, 98:908-913.
68. Schuster M., Silversmith R.E., Bourret R.B. Conformational coupling between the signaling surface and the phosphorylation site in the chemotaxis response regulator CheY. Proc. Natl. Acad. Sci. USA 2001.
69. Bren A., Eisenbach M. How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation. J. Bacteriol. 2000, 182:6865-6873.
70. Moreno M., Audia J.P., Bearson S.M., Webb C., Foster J.W. Regulation of sigma S degradation in Salmonella enterica var typhimurium: In vivo interactions between sigma S, the response regulator MviA(RssB) and ClpX. J. Mol. Microbiol. Biotech. 2000, 2:245-254.
71. Becker G., Klauck E., Hengge-Aronis R. The response regulator RssB, a recognition factor for sigmaS proteolysis in Escherichia coli, can act like an anti-sigmaS factor. Mol. Microbiol. 2000, 35:657-666.
72. Brown J.L., North S., Bussey H. SKN7, a yeast multicopy suppressor of a mutation affecting cell wall b-glucan assembly, encodes a product with domains homologous to prokaryotic two-component regulators and to heat shock transciption factors. J. Bacteriol. 1993, 175:6908-6915.
73. Brown J.M., Firtel R.A. Phosphorelay signalling: New tricks for an ancient pathway. Curr. Biol. 1998, 8:R662-R665.
74. Makino K., Shinagawa H., Amemura M., Kimura S., Nakata A., Ishihama A. Regulation of the phosphate regulon of Escherichia coli: Activation of pstS transcription by PhoB protein in vitro. J. Mol. Biol. 1988, 203:85-95.
75. Winans S.C. Transcriptional induction of an Agrobacterium regulatory gene at tandem promoters by plant-released phenolic compounds, phosphate starvation, and acidic growth media. J. Bacteriol. 1990, 172:2433-2438.
76. Holman T.R., Wu Z., Wanner B.L., Walsh C.T. Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance in Enterococcus faecium. Biochemistry 1994, 33:4625-4631.
77. Mills S.D., Lim C.K., Cooksey D.A. Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae. Mol. Gen. Gene. 1994, 244:341-351.
78. Higgins D.E., DiRita V.J. Genetic analysis of the interaction between Vibrio cholerae transcription activator ToxR and toxT promoter DNA. J. Bacteriol. 1996, 178:1080-1087.
79. Aguirre A., Lejona S., Vescovi E.G., Soncini F.C. Phosphorylated PmrA interacts with the promoter region of ugd in Salmonella enterica serovar typhimurium. J. Bacteriol. 2000, 182:3874-3876. Aguirre A. Lejona S. Vescovi EG. Soncini FC.
80. Makino K., Amemura M., Kim S.-K., Nakata A., Shinagawa H. Role of the s70 subunit of RNA polymerase in transcription activation by activator protein PhoB in Escherichia coli. Genes Dev. 1993, 7:149-160.
81. Kumar A., Grimes B., Fujita N., Makino K., Malloch R.A., Hayward R.S., Ishihama A. Role of sigma70 subunit of Escherichia coli RNA polymerase in transcription activation. J. Mol. Biol. 1994, 235:405-413.
82. Matsuyama S., Mizushima S. Novel rpoA mutation that interferes with the function of OmpR and EnvZ, positive regulators of the ompF and ompC genes that code for the outer-membrane proteins in Escherichia coli K12. J. Mol. Biol. 1987, 195:847-853.
83. Igarashi K., Ishihama A. Bipartite functional map of the E. coli RNA polymerase a subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP. Cell 1991, 65:1015-1022.
84. Slauch J.M., Russo F.D., Silhavy T.J. Suppressor mutations in rpoA suggest that OmpR controls transcription by direct interaction with the alpha subunit of RNA polymerase. J. Bacteriol. 1991, 173:7501-7510.
85. Bowrin V., Brissette R., Tsung K., Inouye M. The a subunit of RNA polymerase specifically inhibits expression of the porin genes ompF and ompC in vivo and in vitro in Escherichia coli. FEMS Microbiol. Lett. 1994, 115:1-6.
86. Pratt L.A., Silhavy T.J. OmpR mutants specifically defective for transcriptional activation. J. Mol. Biol. 1994, 243:579-594.
87. Kondo H., Nakagawa A., Nishihira J., Nishimura Y., Mizuno T., Tanaka I. Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site. Nature Struct. Biol. 1997, 4:28-31.
88. Martinez-Hackert E., Stock A.M. The DNA-binding domain of OmpR: crystal structure of a winged-helix transcription factor. Structure 1997, 5:109-124.
89. Martinez-Hackert E., Stock A.M. Structural relationships in the OmpR family of winged-helix transcription factors. J. Mol. Biol. 1997, 269:301-312.
90. Mizuno T., Tanaka I. Structure of the DNA-binding domain of the OmpR family of response regulators. Mol. Microbiol. 1997, 24:665-667.
91. Okamura H., Hanaoka S., Nagadoi A., Makino K., Nishimura Y. Structural comparison of the PhoB and OmpR DNA-binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box. J. Mol. Biol. 2000, 295:1225-1236.
92. Tyson K.L., Bell A.I., Cole J.A., Busby J.W. Definition of nitrite and nitrate response elements at the anaerobically inducible E. coli nirB promoter: Interactions between FNR and NarL. Mol. Microbiol. 1993, 7:151-157.
93. Li J., Kustu S., Stewart V. In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK, and frdA operon control regions of Escherichia coli K-12. J. Bacteriol. 1994, 241:150-165.
94. Walker M.S., DeMoss J.A. Promoter sequence requirements for Fnr-dependent activation of transcription of the narGHJI operon. Mol. Microbiol. 1991, aa5:353-360.
95. Rabin R.S., Collins L.A., Stewart V. In vivo requirement of integration host factor for nitrate recductase (nar) operon expression in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 1992, 89:8701-8705.
96. Merkel T.J., Dahl J.L., Ebright R.H., Kadner R.J. Transcription activation at the Escherichia coli uhpT promoter by the catabolite gene activator protein. J. Bacteriol. 1995, 177:1712-1718.
97. Baikalov I., Schröder I., Kaczor-Grzeskowiak M., Cascio D., Gunsalus R.P., Dickerson R.E. NarL dimerization? Suggestive evidence from a new crystal form. Biochemistry 1998, 37:3665-3676.
98. Kustu S., North A.K., Weiss D.S. Prokaryyotic transcriptional enhancers and enhancer-binding proteins. Trends Biochem. Sci. 1991, 16:397-402.
99. Weiss V., Claverie-Martin F., Magasanik B. Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription. Proc. Natl. Acad. Sci. USA 1992, 89:5088-5092.
100. Wyman C., Rombel I., North A.K., Bustamente C., Kustu S. Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 1997, 275:1658-1661.
101. Weiss D.S., Batut J., Klose K.E., Keener J., Kustu S. The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription. Cell 1991, 67:155-167.
102. Austin S., Dixon R. The prokaryotic enhancer binding protein NtrC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 1992, 11:2219-2228.
103. Wedel A., Kustu S. The bacterial enhancer-binding protein NtrC is a molecular machine:ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 1995, 9:2042-2052.
104. Osuna J., Soberon X., Morett E. A proposed architecture for the central domain of the bacterial enhancer-binding proteins based on secondary structure prediction and fold recognition. Protein Sci. 1997, 6:543-555.
105. Contreras A., Drummond M. The effect on the function of the transcriptional activator NtrC from K. pneumoniae of mutations in the DNA-recognition helix. Nucleic Acids Res. 1988, 16:4025-4039.
106. Porter S.C., North A.K., Wedel A.B., Kustu S. Oligomerization of NtrC at the glnA enhancer is required for transcriptional activation. Genes Dev. 1993, 7:2258-2273.
107. Pelton J.G., Kustu S., Wemmer D.E. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J. Mol. Biol. 1999, 292:1095-1110.
108. Brennan R.G., Matthews B.W. The helix-turn-helix DNA-binding motif. J. Biol. Chem. 1989, 264:1903-1906.
109. Huala E., Stigter J., Ausubel F.M. The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription. J. Bacteriol. 1992, 174:1428-1431.
110. Drummond M.H., Contreras A., Mitchenall L.A. The function of isolated domains and chimaeric proteins constucted from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae. Mol. Microbiol. 1990, 4:29-37.
111. Tate S., Kato M., Nishimura Y., Arata Y., Mizuno T. Location of DNA-binding segment of a positive regulator, OmpR, involved in activation of the ompF and ompC genes of Escherichia coli. FEBS Lett. 1988, 242:27-30.
112. Simms S.A., Keane M.G., Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J. Biol. Chem. 1985, 260:10161-10168.
113. Anand G.S., Goudreau P.N., Stock A.M. Activation of methylesterase CheB: Evidence of a dual role for the regulatory domain. Biochemistry 1998, 37:14038-14047.
114. Fiedler U., Weiss V. A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules. EMBO J. 1995, 14:3696-3705.
115. Da Re S., Schumacher J., Rousseau P., Fourment J., Ebel C., Kahn D. Phosphorylation-induced dimerisation of the FixJ receiver domain. Mol. Microbiol. 1999, 34:504-511.
116. Harlocker S.L., Bergstrom L., Inouye M. Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli. J. Biol. Chem. 1995, 270:26849-26856.
117. Welch M., Oosawa K., Aizawa S.-I., Eisenbach M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 1993, 90:8787-8791.
118. Li J., Swanson R.V., Simon M.I., Weis R.M. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry 1995, 34:14626-14636.
119. Blat Y., Eisenbach M. Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ. Biochemistry 1994, 33:902-906.
120. Zhu X., Volz K., Matsumura P. The CheZ-binding surface of CheY overlaps the CheA- and FliM-binding surfaces. J. Biol. Chem. 1997, 272:23758-23764.
121. Borkovich K.A., Kaplan N., Hess J.F., Simon M.I. Transmembrane signal transduction in bacterial chemotaxis involves ligand dependent activation of phosphate group transfer. Proc. Natl. Acad. Sci. USA 1989, 86:1208-1212.
122. II, regulates the transcription of the glnALG operon in Escherichia coli. Proc. Natl. Acad. Sci. USA 1986, 83:5909-5913.
123. Aiba H., Mizuno T., Mizushima S. Transfer of phosphoryl group between two regulatory proteins involved in osmoregulatory expression of the ompF and ompC genes in Escherichia coli. J. Biol. Chem. 1989, 264:8563-8567.
124. Lois A.F., Weinstein M., Ditta G.S., Helinski D.R. Autophosphorylation and phosphatase activities of the oxygen-sensing protein FixL of Rhizobium meliloti are coordinately regulated by oxygen. J. Biol. Chem. 1993, 268:4370-4375.
125. Dahl M.K., Msadek T., Kunst F., Rapoport G. The phosphorylation state of the DegU response regulator acts as a molecular switch allowing either degradative enzyme synthesis or expression of genetic competence in Bacillus subtilis. J. Biol. Chem. 1992, 267:14509-14514.
126. Jung K., Tjaden B., Altendorf K. Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli. J. Biol. Chem. 1997, 272:10847-10852.
127. Steed P.M., Wanner B.L. Use of the rep technique for allele replacement to constuct mutants with deletions of the pstSCAB-phoU operon: Evidence of a new role for the PhoU protein in the phosphate regulon. J. Bacteriol. 1993, 175:6797-6809.
128. Wanner B.L. Signal transduction and cross regulation in the Escherichia coli phosphate regulon by PhoR, CreC, and acetyl phosphate. Two-Component Signal Transduction 1995, 203-221. American Society for Microbiology Press, Washington, DC. J.A. Hoch, T.J. Silhavy (Eds.).
129. Goudreau P.N., Lee P.-J., Stock A.M. Stabilization of the phospho-aspartyl residue in a two-component signal transduction system in Thermotoga maritima. Biochemistry 1998, 37:14575-14584.
130. Perego M., Hanstein C., Welsh K.M., Djavakhishvili T., Glaser P., Hoch J.A. Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis. Cell 1994, 79:1047-1055.
131. Ohlsen K.L., Grimsley J.K., Hoch J.A. Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase. Proc. Natl. Acad. Sci. USA 1994, 91:1756-1760.
132. Reizer J., Reizer A., Perego M., Saier M.H. Characterization of a family of bacterial response regulator aspartyl-phosphate (RAP) phosphatases. Microbial Comp. Genet. 1997, 2:103-111.
133. Blat Y., Eisenbach M. Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ: The phosphatase of bacterial chemotaxis. J. Biol. Chem. 1996, 271:1232-1236.
134. Blat Y., Eisenbach M. Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY. J. Biol. Chem. 1996, 271:1226-1231.
135. Da Re S.S., Deville-Bonne.D., Tolstykh T., Veron M., Stock J.B. Kinetics of CheY phosphorylation by small molecule phosphodonors. FEBS Lett. 1999, 457:323-326.
136. Mayover T.L., Halkides C.J., Stewart R.C. Kinetic characterization of CheY phosphorylation reactions: Comparison of P-CheA and small-molecule phosphodonors. Biochemistry 1999, 38:2259-2271.
137. Silversmith R.E., Appleby J.L., Bourret R.B. Catalytic mechanism of phosphorylation and dephosphorylation of CheY: Kinetic characterization of imidazole phosphates as phosphodonors and the role of acid catalysis. Biochemistry 1997, 36:14965-14974.
138. Zapf J.W., Hoch J.A., Whiteley J.M. A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates. Biochemistry 1996, 35:2926-2933.
139. Schuster S.C., Swanson R.V., Alex L.A., Bourret R.B., Simon M.I. Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance. Nature 1993, 365:343-347.
140. Tomomori C., Tanaka T., Dutta R., Park H., Saha S.K., Zhu Y., Ishima R., Liu D., Tong K.I., Kurokawa H., Qian H., Inouye M., Ikura M. Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nature Struct. Biol. 1999, 6:729-734.
141. Zhou H., Dahlquist F.W. Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR. Biochemistry 1997, 36:699-710.
142. Ikegami T., Okada T., Ohki I., Hirayama J., Mizuno T., Shirakawa M. Solution structure and dynamic character of the histidine-containing phosphotransfer domain of anaerobic sensor kinase ArcB from Escherichia coli. Biochemistry 2001, 40:375-386.
143. Kato M., Mizuno T., Shimizu T., Hakoshima T. Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. Cell 1997, 88:717-723.
144. Song H.K., Lee J.Y., Lee M.G., Moon J., Min K., Yang J.K., Suh S.W. Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae. J. Mol. Biol. 1999, 293:753-761.
145. Varughese K.I., Madhusudan, Zhou X.Z., Whiteley J.M., Hoch J.A. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol. Cell. 1998, 2:485-493.
146. Xu Q., West A.H. Conservation of structure and function among histidinecontaining phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1. J. Mol. Biol. 1999, 292:1039-1050.
147. Zapf J., Sen U., Madhusudan, Hoch J.A., Varughese K.I. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Structure Fold Des. 2000, 8:851-862.
148. Knowles J.R. Enzyme-catalyzed phosphoryl transfer reactions. Annu. Rev. Biochem. 1980, 49:877-919.
149. Hess J.F., Bourret R.B., Simon M.I. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 1988, 336:139-143.
150. Swanson R.V., Schuster S.C., Simon M.I. Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities. Biochemistry 1993, 32:7623-7629.
151. Zhou H., Lowry D.F., Swanson R.V., Simon M.I., Dahlquist F.W. NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: Assignments, secondary structure, general fold, and backbone dynamics. Biochemistry 1995, 34:13858-13870.
152. McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc. Natl. Acad. Sci. USA 1998, 95:7333-7338.
153. Stewart R.C., Jahreis K., Parkinson J.S. Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain. Biochemistry 2000, 39:13157-13165.
154. Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nature Struct. Biol. 1998, 5:25-29.
155. Pratt L.A., Silhavy T.J. Porin regulon of Escherichia coli. Two-Component Signal Transduction 1995, 105-127. Am. Soc. Microbiol. Press, Washington, DC. J.A. Hoch, T.J. Silhavy (Eds.).
156. Hoch J.A., Silhavy T.J. Two-Component Signal Transduction 1995, American Society for Microbiology Press, Washington, DC.
157. Aiba H., Nakasai F., Mizushima S., Mizuno T. Evidence for the physiological importance of the phosphotransfer between the two regulatory components, EnvZ and OmpR, in osmoregulation of Escherichia coli. J. Biol. Chem. 1989, 264:14090-14094.
158. Hsing W., Russo F.D., Bernd K.K., Silhavy T.J. Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J. Bacteriol. 1998, 180:4538-4546.
159. Jung K., Altendorf K. Truncation of amino acids 12-128 causes deregulation of the phosphatase activity of the sensor kinase KdpD of Escherichia coli. J. Biol. Chem. 1998, 273:17406-17410.
160. Igo M.M., Ninfa A.J., Stock J.B., Silhavy T.J. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 1989, 3:1725-1734.
161. Kramer G., Weiss V. Functional dissection of the transmitter module of the histidine kinase NtrB in Escherichia coli. Proc. Natl. Acad. Sci. USA 1999, 96:604-609.
162. Walker M.S., DeMoss J.D. Phosphorylation and dephosphorylation catalyzed in vitro by purified components of the nitrate sensing system, NarX and NarL. J. Biol. Chem. 1993, 268:8391-8393.
163. Zhu Y., Qin L., Yoshida T., Inouye M. Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain. Proc. Natl. Acad. Sci. USA 2000, 97:7808-7813.
164. II or NtrB). J. Bacteriol. 1993, 175:7016-7023.
165. Cavicchioli R., Schroder I., Constanti M., Gunsalus R.P. The NarX and NarQ sensor-transmitter proteins of Escherichia coli each require two conserved histidines for nitrate-dependent signal transduction to NarL. J. Bacteriol. 1995, 177:2416-2424.
166. Hsing W., Silhavy T.J. Function of conserved histidine-243 in phosphatase activity of EnvZ, the sensor for porin osmoregulation in Escherichia coli. J. Bacteriol. 1997, 179:3729-3735.
167. II or NtrB), on the phosphatase activity involved in bacterial nitrogen regulation. J. Biol. Chem. 1994, 269:28294-28299.
168. Skarphol K., Waukau J., Forst S.A. Role of His243 in the phosphatase activity of EnvZ in Escherichia coli. J. Bacteriol. 1997, 179:1413-1416.
169. West A.H., Martinez-Hackert E., Stock A.M. Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. J. Mol. Biol. 1995, 250:276-290.