The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait

FEMS Microbiology Reviews

Volumn 22, Issue 4, 1998, Pages 229-253

  Shi, Liang ^a   Potts, Malcolm ^a   Kennelly, Peter J ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

Archaea; Bacteria; Dual specific phosphatase; Protein kinase; Protein phosphatase; Protein tyrosine phosphatase

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE;

ARCHAEOGLOBUS FULGIDUS; BACTERIAL GENE; BORRELIA BURGDORFERI; CYANOBACTERIUM; DATA BASE; DEPHOSPHORYLATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENOME; HAEMOPHILUS INFLUENZAE; HELICOBACTER PYLORI; METHANOBACTERIUM THERMOAUTOTROPHICUM; METHANOCOCCUS JANNASCHII; MYCOPLASMA GENITALIUM; NONHUMAN; PROTEIN PHOSPHORYLATION; REVIEW;

ARCHAEA; ARCHAEOGLOBUS; ARCHAEOGLOBUS FULGIDUS DSM 4304; BACILLUS SUBTILIS; BORRELIA; BORRELIA BURGDORFERI; ESCHERICHIA; ESCHERICHIA COLI K12; EUKARYOTA; HAEMOPHILUS INFLUENZAE; HELICOBACTER; HELICOBACTER PYLORI 26695; METHANOBACTERIUM; METHANOCALDOCOCCUS JANNASCHII; METHANOCOCCUS; METHANOTHERMOBACTER THERMAUTOTROPHICUS; MYCOPLASMA; MYCOPLASMA GENITALIUM G-37; PROKARYOTA; SYNECHOCYSTIS SP.;

EID: 0031764045     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(98)00015-1     Document Type: Article

References (98)

1. Fischer, E.H. and Krebs, E.G. (1989) Commentary on 'The phosphorylase b to a converting enzyme of rabbit skeletal muscle'. Biochim. Biophys. Acta 1000, 297-301.
2. Alex, L.A. and Simon, M.I. (1994) Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet. 10, 133-138.
3. Kennelly, P.J. and Potts, M. (1996) Fancy meeting you here! A fresh look at 'prokaryotic' protein phosphorylation. J. Bacteriol. 178, 4759-4764.
4. Taylor, S.S., Knighton, D.R., Zheng, J., Sowadski, J.M., Gibbs, C.S. and Zoller, M.J. (1993) A template for the protein kinase family. Trends Biochem. Sci. 18, 84-89.
5. Ota, I.M. and Varshavsky, A. (1993) A yeast protein similar to bacterial two-component regulators. Science 262, 566-569.
6. Maeda, T., Wurgler-Murphy, S.M. and Saito, H. (1994) A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369, 242-245.
7. Chang, C., Kwok, S.F., Bleecker, A.B. and Meyerowitz, E.M. (1993) Arabidopsis ethylene-response gene ETR-1: similarity of product to two-component regulators. Science 262, 539-544.
8. Harris, R.A., Popov, K.M., Zhao, Y., Kedishvili, N.Y., Shimomura, Y. and Crabb, D.A. (1995) A new family of protein kinases - the mitochondrial protein kinases. Adv. Enzyme Regul. 35, 147-162.
9. Cozzone, A.J. (1993) ATP-dependent protein kinases in bacteria. J. Cell. Biochem. 51, 7-13.
10. Zhang, C.-C. (1996) Bacterial signalling involving eukaryotic-type protein kinases. Mol. Microbiol. 20, 9-15.
11. Kennelly, P.J. and Potts, M. (1994) Prokaryotic protein phosphatases: reflections of the past. Windows to the future? Adv. Protein Phosphatases 8, 53-68.
12. Cohen, P.T.W. and Cohen, P. (1989) Discovery of a protein phosphatase activity encoded in the genome of bacteriophage λ. Probable identity with open reading frame 221. Biochem. J. 260, 931-934.
13. Guan, K. and Dixon, J.E. (1990) Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249, 553-556.
14. Galyov, E.E., Hakanson, S., Forsberg, A. and Wolf-Watz, H. (1993) A secreted protein kinase of Yersinia pseudotuberculosis is an indipensable virulence determinant. Nature 361, 730-732.
15. Bork, P., Brown, N.P., Hegyi, H. and Schultz, J. (1996) The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci. 5, 1421-1425.
16. Charbonneau, H. and Tonks, N.K. (1992) 1002 protein phosphatases? Annu. Rev. Cell Biol. 8, 463-493.
17. Fauman, E.B. and Saper, M.A. (1996) Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21, 413-417.
18. Hanks, S.K. and Quinn, A.M. (1991) Protein kinase catalytic domain sequences database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62.
19. Koonin, E.V. (1994) Conserved sequences pattern in a wide variety of phosphoesterases. Protein Sci. 3, 356-358.
20. Smith, R.F. and King, K.Y. (1995) Identification of a eukaryotic-like protein kinase gene in Archaebacteria. Protein Sci. 4, 126-129.
21. Patthy, L. (1996) Consensus approaches in detection of distant homologies. Methods Enzymol. 266, 184-198.
22. Klenk, H.P., Clayton, R.A., Tomb, J.F., White, O., Nelson, K.E., Ketchum, K.A., Dodson, R.J., Gwinn, M., Hickey, E.K., Peterson, J.D., Richardson, D.L., Kerlavage, A.R., Graham, D.E., Kyrpides, N.C., Fleischmann, R.D., Quackenbush, J., Lee, N.H., Sutton, G.G., Gill, S., Kirkness, E.F., Dougherty, B.A., McKenney, K., Adams, M.D., Loftus, B., Peterson, S., Reich, C.I., McNeil, L.K., Badger, J.H., Glodek, A., Zhou, L., Overbeek, R., Gocayne, J.D., Weidman, J.F., McDonald, L., Utterback, T., Cotton, M.D., Spriggs, T., Artiach, P., Kaine, B.P., Sykes, S.M., Dadow, P.W., D'Andrea, K.P., Bowman, C., Fujii, C., Garland, S.A., Mason, T.M., Olson, G.J., Fraser, C.M., Smith, H.O., Woese, C.R. and Venter, J.C. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeroglobus fulgidus. Nature 390, 364-379.
23. Kunst, F., Ogasawara, N., Moszer, I., Albertini, A.M., Alloni, G., Azevedo, V., Bertero, M.G., Bessieres, P., Bolotin, A., Borchert, S., Borris, R., Boursier, L., Brans, A., Braun, M., Brignell, S.C., Bron, S., Brouillet, S., Bruschi, C.V., Caldwell, B., Capuano, V., Carter, N.M., Choi, S.K., Codani, J.J., Connerton, I.F., Cummings, N.J., Daniel, R.A., Denizot, F., Devine, K.M., Dusterhoft, A., Ehelich, S.D., Emmerson, P.T., Entian, K.D., Errington, J., Fabret, C., Ferrari, E., Foulger, D., Fritz, C., Fugita, M., Fugita, Y., Fuma, S., Galizzi, A., Galleron, N., Ghim, S.Y., Glaser, P., Goffeau, A., Golightly, E.J., Grandi, G., Guiseppi, G., Guy, B.J., Haga, K., Haiech, J., Harwood, C.R., Henaut, A., Hibert, H., Holsappel, S., Hosono, S., Hullo, M.F., Itaya, M., Jones, L., Joris, B., Karamata, D., Kasahara, Y., Klaerr-Blanchard, M., Klein, C., Kobayashi, Y., Koetter, P., Koningstein, G., Krogh, S., Kumano, M., Kurita, K., Lapidus, A., Lardinois, S., Lauber, J., Lazarevic, V., Lee, S.M., Levine, A., Liu, H., Masuda, S., Mauel, C., Medigue, C., Medina, N., Mellado, R.P., Mizuno, M., Moestl, D., Nakai, S., Noback, M., Noone, D., O'Reilly, M., Ogawa, A., Ogiwara, A., Oudega, B., Park, S.H., Parro, V., Pohl, T.M., Portetelle, D., Porwollik, S., Prescott, A.M., Presecan, E., Pugic, P., Purnelle, B., Rapoport, G., Rey, M., Reynolds, S., Rieger, M., Rivolta, C., Rocha, E., Rose, M., Sadaie, Y., Sato, T., Scanlan, E., Schleich, S., Schroeter, R., Scoffone, F., Sekiguchi, J., Sekowska, A., Serror, P., Shin, B.S., Soldo, B., Sorokin, A., Tacconi, E., Takagi, T., Takahashi, H., Takemaru, K., Takeuchi, M., Tamakoshi, A., Tanaka, T., Terpstra, P., Tognoni, A., Tosato, V., Uchiyama, S., Vandenbol, M., Vannier, F., Vassarotti, A., Viari, A., Wambutt, R., Wedler, E., Wedler, H., Weitzenegger, T., Winters, P., Wipat, A., Yamamoto, H., Yamane, K., Yasumoto, K., Yata, K., Yoshida, K., Yoshikawa, H.F., Zumstein, E., Yoshikawa, H. and Danchin, A. (1997) The complete genome sequence of the gram-positive bacterium Baccillus subtilis. Nature 390, 249-256.
24. Fraser, C.M., Casjens, S., Huang, W.M., Sutton, G.G., Clayton, R., Lathigra, R., White, O., Ketchum, K.A., Dodson, R., Hickey, E.K., Gwinn, M., Dougherty, B., Tomb, J.F., Fleischmann, R.D., Richardson, D., Peterson, J., Kerlavage, A.R., Quackenbush, J., Salzberg, S., Hanson, M., Vugt, R., Palmer, N., Adams, M.D., Gocayne, J., Weidman, J., Utterback, T., Watthey, L., McDonald, L., Artiach, P., Bowman, C., Garland, S., Fujii, C., Cotton, M.D., Horst, K., Roberts, K., Hatch, B., Smith, H.O. and Venter, J.C. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390, 580-590.
25. Blattner, F.R., Plunkett, G. III, Bloch, C.A., Perna, N.T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J.D., Rode, C.K., Mayhew, G.F., Gregor, J., Davis, N.W., Kirkpatrick, H.A., Goeden, M.A., Rose, D.J., Mau, B. and Shao, Y. (1997) The complete genome sequence of Escherichia coli K-12. Science 277, 1453-1462.
26. Fleischmann, R.D., Adams, M.D., White, O., Clayton, R.A., Kirkness, E.F., Kerlavage, A.R., Bult, C.J., Tomb, J.F., Dougherty, B.A., Merrick, J.M., McKenney, K., Sutton, G., FitzHugh, W., Fields, C., Gocayne, J.D., Scott, J., Shirley, R., Liu, L., Glodek, A., Kelley, J.M., Weidman, J.F., Phillips, C.A., Spriggs, T., Hedblom, E., Cotton, M.D., Utterback, T.R., Hanna, M.C., Nguyen, D.T., Saudek, D.M., Brandon, R.C., Fine, L.D., Fritchman, J.L., Fuhrmann, J.L., Geoghagen, N.S.M., Gnehm, C.L., McDonald, L.A., Small, K.V., Fraser, C.M., Smith, H.O. and Venter, J.C. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512.
27. Tomb, J.F., White, O., Kerlavage, A.R., Clayton, R.A., Sutton, G.G., Fleischmann, R.D., Ketchum, K.A., Klenk, H.P., Gill, S., Dougherty, B.A., Nelson, K., Quackenbush, J., Zhou, L., Kirkness, E.F., Peterson, S., Loftus, B., Richardson, D., Dodson, R., Khalak, H.G., Glodek, A., Mckenney, K., Fitzgerald, L.M., Lee, N., Adams, M.D., Hickey, E.K., Berg, D.E., Gocayne, J.D., Utterback, T.R., Peterson, J.D., Kelly, J.M., Cotton, M.D., Weidman, J.M., Fujii, C., Bowman, C., Watthey, L., Wallin, E., Hayes, W.S., Borodovsky, M., Karp, P.D., Smith, H.O., Fraser, C.M. and Venter, J.C. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388, 539-547.
28. Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T., Bashirzadeh, R., Blakely, D., Cook, R., Gilbert, K., Harrison, D., Hoang, L., Keagle, P., Lumm, W., Pothier, B., Qiu, D., Spadafora, R., Vicaire, R., Wang, Y., Wierzbowski, J., Gibson, R., Jiwani, N., Caruso, A., Bush, D., Safer, H., Patwell, D., Prabhakar, S., McDougall, S., Shimer, G., Goyal, A., Pietrokovski, S., Church, G.M., Daniels, C.J., Mao, J.I., Rice, P., Nolling, J. and Reeve, J.N. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum H: fuctional analysis and comparative genomics. J. Bacteriol. 179, 7135-7155.
29. Bult, C.J., White, O., Olsen, G.J., Zhou, L., Fleischmann, R.D., Sutton, G.G., Blake, J.A., Fitzgerald, L.M., Clayton, R.A., Gocayne, J.D., Kerlavage, A.R., Dougherty, B.A., Tomb, J.F., Adams, M.D., Reich, C.I., Kirkness, E.F., Weinstock, K.G., Merrick, J.M., Glodek, A., Scott, J.L., Geoghagen, N.S.M. and Venter, J.C. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073.
30. Fraser, C.M., Gocayne, J.D., White, O., Adams, M.D., Clayton, R.A., Fleischmann, R.D., Bult, C.J., Kerlavage, A.R., Sutton, G., Kelley, J.K., Fritchman, J.L., Weidman, J.F., Small, K.V., Sandusky, M., Furhrmann, J., Nguyen, D., Utterback, T.R., Saudek, D.M., Phillips, C.A., Merrick, J.M., Tomb, J.F., Dougherty, B.A., Bott, K.F., Hu, P.C., Lucier, T.S., Peterson, S.N., Smith, H.O., Hutchison, C.A. III and Venter, J.C. (1995) The minimal gene complement of Mycoplasma genitalium. Science 270, 397-403.
31. Kaneto, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., Miyajima, N., Hirpsawa, M., Sugiura, M., Sasamoto, S., Kimura, T., Hosouchi, T., Matsuno, A., Muraki, A., Nakazaki, N., Naruo, K., Okumura, S., Shimpo, S., Takeuchi, C., Wada, T., Watanaba, A., Yamada, M., Yasuda, M. and Tabata, S. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 30, 109-136.
32. Johnson, M. (1996) Genome sequencing: The complete code for a eukaryotic cell. Curr. Biol. 6, 500-503.
33. Hanks, S.K. and Hunter, T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
34. Bray, D. (1995) Protein molecules as computational elements in living cells. Nature 376, 307-312.
35. Marks, F. (1996) The brain of the cell. In: Protein Phosphorylation (Marks, F., Ed.), pp. 1-35. VCH, New York, NY.
36. Knighton, D.R., Zheng, J., Ten Eyck, L.F., Ashford, V.A., Xuong, N.-H., Taylor, S.S. and Sowadski, J.M. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
37. Knighton, D.R., Zheng, J., Ten Eyck, L.F., Xuong, N.-H., Taylor, S.S. and Sowadski, J.M. (1991) Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420.
38. Brenner, S. (1988) Phosphotransferase sequence homology. Nature 329, 21.
39. Heinzel, P., Worbitzky, O., Distler, J. and Piepersberg, W. (1988) A second streptomycin resistance gene from Streptomyces griseus codes for streptomycin-3″-phosphotransferase. Relationships between antibiotic and protein kinases. Arch. Microbiol. 150, 184-192.
40. Martin, P., Jullien, E. and Courvalin, P. (1988) Nucleotide sequence of Acinetobacter baumannii aphA-6 gene: Evolutionary and functional implications of sequence homologies with nucleotide-binding proteins, kinases and other aminoglycoside-modifying enzymes. Mol. Microbiol. 2, 615-625.
41. Hon, W.-C., McKay, G.A., Thompson, P.R., Sweet, R.M., Yang, D.S.C., Wright, G.D. and Berghius, A.M. (1997) Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89, 887-895.
42. Skorko, R. (1989) Polyphosphate as a source of phosphoryl group in protein modification in the archaebacterium Sulfolobus acidocaldarius. Biochimie 71, 1089-1093.
43. Barford, D. (1996) Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem. Sci. 21, 407-412.
44. Mumby, M.C. and Walter, G. (1993) Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol. Rev. 73, 673-699.
45. Shenolikar, S. (1994) Protein serine/threonine phosphatases -new avenues for cell regulation. Annu. Rev. Cell Biol. 10, 55-86.
46. Schreiber, S.L. (1992) Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell 70, 365-368.
47. Hubbard, M.J. and Cohen, P. (1993) On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 18, 172-177.
48. Barton, G.J., Cohen, P.T.W. and Barford, D. (1994) Conservation analysis and structure prediction of the protein serine/ threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases. Eur. J. Biochem. 220, 225-237.
49. Missiakas, D. and Raina, S. (1997) Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB. EMBO J. 16, 1670-1685.
50. Lohse, D.L., Denu, J.M. and Dixon, J.E. (1995) Insights derived from the structures of the Ser/Thr phosphatases calcineurin and protein phosphatase 1. Structure 3, 987-990.
51. Shi, L. and Carmichael, W.W. (1997) ppl-cyano2, a protein serine/threonine phosphatase 1 gene from the cyanobacterium Microcystis aeruginosa UTEX 2063. Arch. Microbiol. 168, 528-531.
52. Leng, J., Cameron, A.J., Buckel, S. and Kennelly, P.J. (1995) Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon. J. Bacteriol. 177, 6510-6517.
53. Solow, B., Young, J.C., White, R.H. and Kennelly, P.J. (1997) Gene cloning and expression and characterization of a toxin-sensitive protein phosphatase from the methanogenic archaeon Methanosarcina thermophila TM-1. J. Bacteriol. 179, 5072-5075.
54. Cohen, P.T.W., Collins, J.F., Coulson, A.F.W., Berndt, N. and da Cruz e Silva, O.B. (1988) Segments of bacteriophage λ (orf 221) and φ80 are homologous to genes encoding for mammalian protein phosphatases. Gene 69, 131-134.
55. Zhou, S., Clemens, J.C., Hakes, D.J., Barford, D. and Dixon, J.E. (1993) Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. J. Biol. Chem. 268, 17754-17761.
56. Das, A.K., Helps, N.R., Cohen, P.T.W. and Barford, D. (1996) Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. EMBO J. 15, 6798-6809.
57. Duncan, L., Alper, S., Arigoni, F., Losick, R. and Stragier, P. (1995) Activation of cell specific transcription by a serine phosphatase at the site of asymmetric division. Science 270, 641-644.
58. Yang, X., Kang, C.M., Brody, M.S. and Price, C.W. (1996) Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 10, 2265-2275.
59. Adler, E., Donella-Deana, A., Arigoni, F., Pinna, L.A. and Stragier, P. (1997) Structural relationship between a bacterial developmental protein and eukaryotic PP2C protein phosphatases. Mol. Microbiol. 23, 57-62.
60. Khvorova, A., Zhang, L., Higgins, M.L. and Piggot, P.J. (1998) The spoIIE locus is involved in the Spo0A-dependent switch in the location of the FtsZ rings in Bacillus subtilis. J. Bacteriol. 180, 1256-1260.
61. B in response to environmental signals. J. Bacteriol. 177, 123-133.
62. r phosphotyrosine protein phosphatases. Evidence for a long evolutionary history. Int. J. Biochem. Cell Biol. 29, 279-292.
63. Guan, K. and Dixon, J.E. (1991) Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266, 17026-17030.
64. 124 in the dual specificity phosphatase VHR. J. Biol. Chem. 269, 28084-28090.
65. Eckstein, J.W., Beer-Romero, P. and Berdo, I. (1996) Identification of an essential acidic residue in Cdc25 protein phosphatase and a general three-dimensional model for a core region in protein phosphatases. Protein Sci. 5, 5-12.
66. Jia, Z., Barford, D., Flint, A.J. and Tonks, N.K. (1995) Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 268, 1754-1758.
67. Pannifer, A.D.B., Flint, A.J., Tonks, N.K. and Barford, D. (1998) Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography. J. Biol. Chem. 273, 10454-10462.
68. Zhang, Z.-Y. and Dixon, J.E. (1993) Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of conserved histidine 402. Biochemistry 32, 9340-9345.
69. Denu, J.M. and Dixon, J.E. (1995) A catalytic mechanism for the dual-specific phosphatases. Proc. Natl. Acad. Sci. USA 92, 5910-5914.
70. Potts, M., Sun, H., Mockaitis, K., Kennelly, P.J., Reed, D. and Tonks, N. K. (1993) A protein-tyrosine/serine phosphatase encoded by the genome of the cyanobacterium Nostoc Commune UTEX 584. J. Biol. Chem. 268, 7632-7635.
71. Howell, L.D., Griffiths, C., Slade, L.W., Potts, M. and Kennelly, P.J. (1996) Substrate specificity of IphP, a cyanobacterial dual-specificity protein phosphatase with MAP kinase phosphatase activity. Biochemistry 35, 7566-7572.
72. Kaniga, K., Uralil, J., Bliska, J.B. and Galan, J.E. (1996) A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol. Microbiol. 21, 633-641.
73. Bliska, J.B., Guan, K., Dixon, J.E. and Falkow, S. (1991) Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc. Natl. Acad. Sci. USA 88, 1187-1191.
74. Fu, Y. and Galan, J.E. (1998) The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Mol. Microbiol. 27, 359-368.
75. Li, Y. and Strohl, W.R. (1996) Cloning, purification, and properties of a phosphotyrosine phosphatase from Streptomyces coelicolor A3(2). J. Bacteriol. 178, 136-142.
76. Grangeasse, C., Doublet, P., Vincent, C., Vaganay, E., Riberty, M., Duclos, B. and Cozzone, A.J. (1998) Functional characterization of the low-molecular-mass phosphotyrosine-protein phosphatase of Acinetobacter johnsonii. J. Mol. Biol. 278, 339-347.
77. Takagi, T., Moore, C.R., Diehn, F. and Buratowski, S. (1997) An RNA 5′-triphosphatase related to the protein tyrosine phosphatases. Cell 89, 867-873.
78. Takemura, K.-I., Mizuno, M., Sato, T., Takeuchi, M. and Kobayashi, Y. (1995) Complete nucleotide sequence of a skin element excised by DNA rearrangement during sporulation in Bacillus subtilis. Microbiology 141, 323-327.
79. Gladysheva, T.B., Oden, K.L. and Posen, B.P. (1994) Properties of the arsenate reductase of plasmid R773. Biochemistry 33, 7288-7293.
80. Ji, G., Garber, E.A.E., Armes, L.G., Chen, C-H., Fuchs, J.A. and Silver, S. (1994) Arsenate reductase of Staphylocccus aureus plasmid pI258. Biochemistry 33, 7294-7299.
81. Diorio, C., Cai, J., Marmor, J., Shinder, R. and Dubow, M.S. (1995) An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria. J. Bacteriol. 177, 2050-2056.
82. Ji, G. and Silver, S. (1992) Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258. J. Bacteriol. 174, 3684-3694.
83. Rosenstein, R., Peschel, A., Wieland, B. and Gotz, F. (1992) Expression and regulation of the antimonite, arsenite, and arsenate resistance operon of Staphylococcus xylosus plasmid pSX267. J. Bacteriol. 174, 3676-3683.
84. Liu, J., Gladysheva, T.B., Lee, L. and Posen, B.P. (1995) Identification of an essential cysteine residue in the ArsC arsenate reductase of plasmid R773. Biochemistry 34, 13472-13476.
85. Gladysheva, T., Liu, J. and Posen, B.P. (1996) His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773. J. Biol. Chem. 271, 33256-33260.
86. Bobrowicz, P., Wysocki, R., Owsianik, G., Goffeau, A. and Ulaszewski, S. (1997) Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae. Yeast 13, 819-828.
87. Russell, P., Moreno, S. and Reed, S.I. (1989) Conservation of mitotic controls in fission and budding yeasts. Cell 57, 295-303.
88. Himmelreich, R., Hilbert, H., Plagens, H., Pirkl, E., Li, B.C. and Herrmann, R. (1996) Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res. 24, 4420-4449.
89. Av-Gay, Y. and Davies, J. (1997) Components of eukaryotic-like protein signaling pathways in Mycobacterium tuberculosis. Microb. Comp. Genomics 2, 63-73.
90. Cortay, J.-C., Bleicher, F., Rieul, C., Reeves, H.C. and Cozzone, A.J. (1988) Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli. J. Bacteriol. 170, 89-97.
91. Fischer, C., Geourjon, C., Bourson, C. and Deutscher, J. (1996) Cloning and characterization of the Bacillus subtilis prkA gene encoding a novel serine protein kinase. Gene 168, 55-60.
92. Galinier, A., Kravanja, M., Engelmann, R., Hengstenberg, W., Kilhoffer, M.-C., Deutscher, J. and Haiech, J. (1998) New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression. Proc. Natl. Acad. Sci. USA 95, 1823-1828.
93. Reizer, J., Hoischen, C., Titgemeyer, F., Rivolta, C., Rabus, R., Stulke, J., Karamata, D., Saier, M.H. Jr. and Hillen, W. (1998) A novel protein kinase that controls carbon catabolite repression in bacteria. Mol. Microbiol. 27, 1157-1169.
94. Min, K.-T., Hilditch, C.M., Diederich, B., Errington, J. and Yudkin, M.D. (1993) Sigma F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-sigma factor that is also a protein kinase. Cell 74, 735-742.
95. Koretke, K.K., Warren, P.V., Walters, S., Lupas, A.N. and Brown, J.R. (1998) A study of the evolution of genes and genomes through multiple genome comparisons: an example involving the two-component signal transduction pathway. Microbial Comp. Genomics 3, 79.
96. Kim, Y., Huang, J., Cohen, P. and Matthews, H.R. (1993) Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases. J. Biol. Chem. 268, 18513-18518.
97. Guan, K., Broyles, S.S. and Dixon, J.E. (1991) A tyr/ser protein phosphatase encoded by vaccinia virus. Nature 350, 359-362.
98. Matsumoto, A., Hong, S.-K., Ishizuka, H., Horinouchi, S. and Beppu, T. (1994) Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase. Gene 146, 47-56.