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Volumn 148, Issue 10, 2002, Pages 3277-3284

A novel mode of control of Mycoplasma pneumoniae HPr kinase/phosphatase activity reflects its parasitic lifestyle

Author keywords

Catabolite repression; Mutagenesis; Phosphorylation; Walker A box

Indexed keywords

ADENOSINE TRIPHOSPHATE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN KINASE; REGULATOR PROTEIN;

EID: 0036773364     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-148-10-3277     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0034663605 scopus 로고    scopus 로고
    • Proteomics of Mycoplasma genitalium: Identification and characterization of unannotated and atypical proteins in a small model genome
    • Balasubramanian, S., Schneider, T., Gerstein, M. & Regal, L. (2000). Proteomics of Mycoplasma genitalium: identification and characterization of unannotated and atypical proteins in a small model genome. Nucleic Acids Res 28, 3075-3082.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3075-3082
    • Balasubramanian, S.1    Schneider, T.2    Gerstein, M.3    Regal, L.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0032891071 scopus 로고    scopus 로고
    • The HPr(Ser) kinase of Streptococcus salivarius: Purification, properties, and cloning of the hprK gene
    • Brochu, D. & Vadeboncoeur, C. (1999). The HPr(Ser) kinase of Streptococcus salivarius: purification, properties, and cloning of the hprK gene. J Bacteriol 181, 709-717.
    • (1999) J. Bacteriol , vol.181 , pp. 709-717
    • Brochu, D.1    Vadeboncoeur, C.2
  • 4
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
    • Deutscher, J., Küster, E., Bergstedt, U., Charrier, V. & Hillen, W. (1995). Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol Microbiol 15, 1049-1053.
    • (1995) Mol. Microbiol , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Küster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 5
    • 0033996770 scopus 로고    scopus 로고
    • Phosphorylation of HPr by the bifunctional HPr Kinase/P-ser-HPr phosphatase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion
    • Dossonnet, V., Monedero, V., Zagorec, M., Galinier, A., Perez-Martinez, G. & Deutscher, J. (2000). Phosphorylation of HPr by the bifunctional HPr Kinase/P-ser-HPr phosphatase from Lactobacillus casei controls catabolite repression and inducer exclusion but not inducer expulsion. J Bacteriol 182, 2582-2590.
    • (2000) J. Bacteriol , vol.182 , pp. 2582-2590
    • Dossonnet, V.1    Monedero, V.2    Zagorec, M.3    Galinier, A.4    Perez-Martinez, G.5    Deutscher, J.6
  • 6
    • 0023052316 scopus 로고
    • 31P-NMR studies of Mycoplasma gallisepticum cells using a continuous perfusion technique
    • 31P-NMR studies of Mycoplasma gallisepticum cells using a continuous perfusion technique. FEBS Lett 204, 373-376.
    • (1986) FEBS Lett , vol.204 , pp. 373-376
    • Egan, W.1    Barile, M.2    Rottem, S.3
  • 8
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • 26 other authors
    • Fraser, C. M., Gocayne, J. D., White, O. & 26 other authors (1995). The minimal gene complement of Mycoplasma genitalium. Science 270, 397-403.
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1    Gocayne, J.D.2    White, O.3
  • 11
    • 0035987277 scopus 로고    scopus 로고
    • HPr kinase/phosphatase of Bacillus subtilis: Expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression
    • Hanson, K. G., Steinhauer, K., Reizer, J., Hillen, W. & Stülke, J. (2002). HPr kinase/phosphatase of Bacillus subtilis: expression of the gene and effects of mutations on enzyme activity, growth and carbon catabolite repression. Microbiology 148, 1805-1811.
    • (2002) Microbiology , vol.148 , pp. 1805-1811
    • Hanson, K.G.1    Steinhauer, K.2    Reizer, J.3    Hillen, W.4    Stülke, J.5
  • 13
    • 0030811859 scopus 로고    scopus 로고
    • Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium
    • Himmelreich, R., Plagens, H., Hilbert, H., Reiner, B. & Herrmann, R. (1997). Comparative analysis of the genomes of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium. Nucleic Acids Res 25, 701-712.
    • (1997) Nucleic Acids Res , vol.25 , pp. 701-712
    • Himmelreich, R.1    Plagens, H.2    Hilbert, H.3    Reiner, B.4    Herrmann, R.5
  • 14
    • 0027423247 scopus 로고
    • Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii
    • Hoischen, C., Dijkstra, A., Rottem, S., Reizer, J. & Saier, M. H., Jr (1993). Presence of protein constituents of the gram-positive bacterial phosphotransferase regulatory system in Acholeplasma laidlawii. J Bacteriol 175, 6599-6604.
    • (1993) J. Bacteriol , vol.175 , pp. 6599-6604
    • Hoischen, C.1    Dijkstra, A.2    Rottem, S.3    Reizer, J.4    Saier M.H., Jr.5
  • 16
    • 0034023216 scopus 로고    scopus 로고
    • Characterization of an HPr kinase mutant of Staphylococcus xylosus
    • Huynh, P. L., Jankovic, I., Schnell, N. F. & Brückner, R. (2000). Characterization of an HPr kinase mutant of Staphylococcus xylosus. J Bacteriol 182, 1895-1902.
    • (2000) J. Bacteriol , vol.182 , pp. 1895-1902
    • Huynh, P.L.1    Jankovic, I.2    Schnell, N.F.3    Brückner, R.4
  • 17
    • 0026573219 scopus 로고
    • Isocitrate dehydrogenase kinase/phosphatase: Identification of mutations which selectively inhibit phosphatase activity
    • Ikeda, T. P., Houtz, E. & LaPorte, D. C. (1992). Isocitrate dehydrogenase kinase/phosphatase: identification of mutations which selectively inhibit phosphatase activity. J Bacteriol 174, 1414-1416.
    • (1992) J. Bacteriol , vol.174 , pp. 1414-1416
    • Ikeda, T.P.1    Houtz, E.2    LaPorte, D.C.3
  • 18
    • 0034695574 scopus 로고    scopus 로고
    • The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding
    • Jault, J. M., Fieulaine, S., Nessler, S., Gonzalo, P., Di Pietro, A., Deutscher, J. & Galinier, A. (2000). The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding. J Biol Chem 275, 1773-1780.
    • (2000) J. Biol. Chem , vol.275 , pp. 1773-1780
    • Jault, J.M.1    Fieulaine, S.2    Nessler, S.3    Gonzalo, P.4    Di Pietro, A.5    Deutscher, J.6    Galinier, A.7
  • 20
    • 0019476463 scopus 로고
    • The importance of inorganic phosphate in regulation of energy metabolism of Streptococcus lactis
    • Mason, P. W., Carbone, D. P., Cushman, R. A. & Waggoner, A. S. (1981). The importance of inorganic phosphate in regulation of energy metabolism of Streptococcus lactis. J Biol Chem 256, 1861-1866.
    • (1981) J. Biol. Chem , vol.256 , pp. 1861-1866
    • Mason, P.W.1    Carbone, D.P.2    Cushman, R.A.3    Waggoner, A.S.4
  • 21
    • 0026697738 scopus 로고
    • Catabolism in mollicutes
    • Miles, R. J. (1992). Catabolism in mollicutes. J Gen Microbiol 138, 1773-1783.
    • (1992) J. Gen. Microbiol , vol.138 , pp. 1773-1783
    • Miles, R.J.1
  • 23
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin, S., Yogev, D. & Naot, Y. (1998). Molecular biology and pathogenicity of mycoplasmas. Microbiol Mol Biol Rev 62, 1094-1156.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 26
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding, proteins
    • Saraste, M., Sibbald, P. R. & Wittinghofer, A. (1990). The P-loop - a common motif in ATP- and GTP-binding, proteins. Trends Biochem Sci 15, 430-434.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 27
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 28
    • 0031039255 scopus 로고    scopus 로고
    • Expression, inducer spectrum, domain structure, and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250
    • Schirmer, F., Ehrt, S. & Hillen, W. (1997). Expression, inducer spectrum, domain structure, and function of MopR, the regulator of phenol degradation in Acinetobacter calcoaceticus NCIB8250. J Bacteriol 179, 1329-1336.
    • (1997) J. Bacteriol , vol.179 , pp. 1329-1336
    • Schirmer, F.1    Ehrt, S.2    Hillen, W.3
  • 29
    • 0036006275 scopus 로고    scopus 로고
    • Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae
    • Steinhauer, K., Allen, G. S., Hillen, W., Stülke, J. & Brennan, R. G. (2002). Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallogr Sect D 58, 515-518.
    • (2002) Acta Crystallogr. Sect. D , vol.58 , pp. 515-518
    • Steinhauer, K.1    Allen, G.S.2    Hillen, W.3    Stülke, J.4    Brennan, R.G.5
  • 30
    • 0024405978 scopus 로고
    • Mutation of the predicted ATP binding site inactivates both activities of isocitrate dehydrogenase/phosphatase
    • Stueland, C. S., Ikeda, T. P. & LaPorte, D. C. (1989). Mutation of the predicted ATP binding site inactivates both activities of isocitrate dehydrogenase/phosphatase. J Biol Chem 264, 13775-13779.
    • (1989) J. Biol. Chem , vol.264 , pp. 13775-13779
    • Stueland, C.S.1    Ikeda, T.P.2    LaPorte, D.C.3
  • 31
    • 0033118267 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria
    • Stülke, J. & Hillen, W. (1999). Carbon catabolite repression in bacteria. Curr Opin Microbiol 2, 195-201.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 195-201
    • Stülke, J.1    Hillen, W.2
  • 32
    • 0029941304 scopus 로고    scopus 로고
    • The ATP-binding site in the 2-kinase domain of liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
    • Vertommen, D., Bertrand, L., Sontag, B., Di Pietro, A., Louckx, M. P., Vidal, H., Hue, L. & Rider, M. H. (1996). The ATP-binding site in the 2-kinase domain of liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. J Biol Chem 271, 17875-17880.
    • (1996) J. Biol. Chem , vol.271 , pp. 17875-17880
    • Vertommen, D.1    Bertrand, L.2    Sontag, B.3    Di Pietro, A.4    Louckx M., P.5    Vidal, H.6    Hue, L.7    Rider, M.H.8
  • 33
    • 0033768687 scopus 로고    scopus 로고
    • Sugar uptake and carbon catabolite repression in Bacillus megaterium strains with inactivated ptsHI
    • Wagner, A., Küster-Schöck, E. & Hillen, W. (2000). Sugar uptake and carbon catabolite repression in Bacillus megaterium strains with inactivated ptsHI. J Mol Microbiol Biotechnol 2, 587-592.
    • (2000) J. Mol. Microbiol. Biotechnol , vol.2 , pp. 587-592
    • Wagner, A.1    Küster-Schöck, E.2    Hillen, W.3
  • 34
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. (1982). Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 35
    • 0000784165 scopus 로고    scopus 로고
    • The proteome of Mycoplasma genitalium: Chaps-soluble component
    • Wasinger, V. C., Pollack, J. D. & Humphery-Smith, I. (2000). The proteome of Mycoplasma genitalium: Chaps-soluble component. Eur J Biochem 267, 1571-1582.
    • (2000) Eur. J. Biochem , vol.267 , pp. 1571-1582
    • Wasinger, V.C.1    Pollack, J.D.2    Humphery-Smith, I.3
  • 37
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. (1987). Bacterial evolution. Microbiol Rev 51, 221-271.
    • (1987) Microbiol. Rev , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 39
    • 0032566324 scopus 로고    scopus 로고
    • Topography of the interaction of HPr(Ser) kinase with HPr
    • Zhu, P.-P., Herzberg, O. & Peterkofsky, A. (1998). Topography of the interaction of HPr(Ser) kinase with HPr. Biochemistry 37, 11762-11770.
    • (1998) Biochemistry , vol.37 , pp. 11762-11770
    • Zhu, P.-P.1    Herzberg, O.2    Peterkofsky, A.3


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