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Volumn 87, Issue 4, 2013, Pages 769-788

Stoichiometry and perturbation studies of the LiaFSR system of Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

LIAF PROTEIN; LIAR PROTEIN; LIAS PROTEIN; MEMBRANE PROTEIN; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG;

EID: 84873433178     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12130     Document Type: Article
Times cited : (46)

References (54)
  • 1
    • 1942443703 scopus 로고    scopus 로고
    • The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator
    • Albanesi, D., Mansilla, M.C., and de Mendoza, D. (2004) The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator. J Bacteriol 186: 2655-2663.
    • (2004) J Bacteriol , vol.186 , pp. 2655-2663
    • Albanesi, D.1    de Mansilla, M.C.2    Mendoza, D.3
  • 2
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • Arnaud, M., Chastanet, A., and Debarbouille, M. (2004) New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl Environ Microbiol 70: 6887-6891.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3
  • 3
    • 0037457896 scopus 로고    scopus 로고
    • Robustness and the cycle of phosphorylation and dephosphorylation in a two-component regulatory system
    • Batchelor, E., and Goulian, M. (2003) Robustness and the cycle of phosphorylation and dephosphorylation in a two-component regulatory system. Proc Natl Acad Sci USA 100: 691-696.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 691-696
    • Batchelor, E.1    Goulian, M.2
  • 4
    • 45549091606 scopus 로고    scopus 로고
    • A close-up view of the VraSR two-component system. A mediator of Staphylococcus aureus response to cell wall damage
    • Belcheva, A., and Golemi-Kotra, D. (2008) A close-up view of the VraSR two-component system. A mediator of Staphylococcus aureus response to cell wall damage. J Biol Chem 283: 12354-12364.
    • (2008) J Biol Chem , vol.283 , pp. 12354-12364
    • Belcheva, A.1    Golemi-Kotra, D.2
  • 5
    • 0030843812 scopus 로고    scopus 로고
    • CCR: a rapid and simple approach for mutation detection
    • Bi, W., and Stambrook, P.J. (1997) CCR: a rapid and simple approach for mutation detection. Nucleic Acids Res 25: 2949-2951.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2949-2951
    • Bi, W.1    Stambrook, P.J.2
  • 6
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in Escherichia coli
    • Cai, S.J., and Inouye, M. (2002) EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J Biol Chem 277: 24155-24161.
    • (2002) J Biol Chem , vol.277 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 7
    • 0002301028 scopus 로고
    • Genetic analysis
    • Harwood, C.R., and Cutting, S.M. (eds). Chichester, UK: John Wiley & Sons.
    • Cutting, S.M., and Van der Horn, P.B. (1990) Genetic analysis. In Molecular Biological Methods for Bacillus. Harwood, C.R., and Cutting, S.M. (eds). Chichester, UK: John Wiley & Sons, pp. 27-74.
    • (1990) Molecular Biological Methods for Bacillus , pp. 27-74
    • Cutting, S.M.1    Van der Horn, P.B.2
  • 8
    • 22644441730 scopus 로고    scopus 로고
    • The phage-shock-protein response
    • Darwin, A.J. (2005) The phage-shock-protein response. Mol Microbiol 57: 621-628.
    • (2005) Mol Microbiol , vol.57 , pp. 621-628
    • Darwin, A.J.1
  • 9
    • 0033735885 scopus 로고    scopus 로고
    • The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37°C
    • Derre, I., Rapoport, G., and Msadek, T. (2000) The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37°C. Mol Microbiol 38: 335-347.
    • (2000) Mol Microbiol , vol.38 , pp. 335-347
    • Derre, I.1    Rapoport, G.2    Msadek, T.3
  • 10
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: how one organism sees its world
    • Fabret, C., Feher, V.A., and Hoch, J.A. (1999) Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J Bacteriol 181: 1975-1983.
    • (1999) J Bacteriol , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 12
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao, R., and Stock, A.M. (2009) Biological insights from structures of two-component proteins. Annu Rev Microbiol 63: 133-154.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 13
    • 1842558252 scopus 로고    scopus 로고
    • Robust control in bacterial regulatory circuits
    • Goulian, M. (2004) Robust control in bacterial regulatory circuits. Curr Opin Microbiol 7: 198-202.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 198-202
    • Goulian, M.1
  • 14
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A.M., Shazand, K., Frandsen, N., and Stragier, P. (1995) Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167: 335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 15
    • 65649154706 scopus 로고    scopus 로고
    • Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin
    • Hachmann, A.-B., Angert, E.R., and Helmann, J.D. (2009) Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin. Antimicrob Agents Chemother 53: 1598-1609.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1598-1609
    • Hachmann, A.-B.1    Angert, E.R.2    Helmann, J.D.3
  • 16
    • 51149117340 scopus 로고    scopus 로고
    • The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP
    • Heinrich, J., Lunden, T., Kontinen, V., and Wiegert, T. (2008) The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP. Microbiology 154: 1989-1997.
    • (2008) Microbiology , vol.154 , pp. 1989-1997
    • Heinrich, J.1    Lunden, T.2    Kontinen, V.3    Wiegert, T.4
  • 17
    • 33645050677 scopus 로고    scopus 로고
    • The vancomycin resistance VanRS two-component signal transduction system of Streptomyces coelicolor
    • Hutchings, M.I., Hong, H.J., and Buttner, M.J. (2006) The vancomycin resistance VanRS two-component signal transduction system of Streptomyces coelicolor. Mol Microbiol 59: 923-935.
    • (2006) Mol Microbiol , vol.59 , pp. 923-935
    • Hutchings, M.I.1    Hong, H.J.2    Buttner, M.J.3
  • 18
    • 78650506427 scopus 로고    scopus 로고
    • Conserved mechanism for sensor phosphatase control of two-component signaling revealed in the nitrate sensor NarX
    • Huynh, T.N., Noriega, C.E., and Stewart, V. (2010) Conserved mechanism for sensor phosphatase control of two-component signaling revealed in the nitrate sensor NarX. Proc Natl Acad Sci USA 107: 21140-21145.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21140-21145
    • Huynh, T.N.1    Noriega, C.E.2    Stewart, V.3
  • 19
    • 18844397802 scopus 로고    scopus 로고
    • Transcriptome analysis of the secretion stress response of Bacillus subtilis
    • Hyyryläinen, H.L., Sarvas, M., and Kontinen, V. (2005) Transcriptome analysis of the secretion stress response of Bacillus subtilis. Appl Microbiol Biotechnol 67: 389-396.
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 389-396
    • Hyyryläinen, H.L.1    Sarvas, M.2    Kontinen, V.3
  • 20
    • 33745923792 scopus 로고    scopus 로고
    • Regulation of LiaRS-dependent gene expression in Bacillus subtilis: identification of inhibitor proteins, regulator binding sites and target genes of a conserved cell envelope stress-sensing two-component system
    • Jordan, S., Junker, A., Helmann, J.D., and Mascher, T. (2006) Regulation of LiaRS-dependent gene expression in Bacillus subtilis: identification of inhibitor proteins, regulator binding sites and target genes of a conserved cell envelope stress-sensing two-component system. J Bacteriol 188: 5153-5166.
    • (2006) J Bacteriol , vol.188 , pp. 5153-5166
    • Jordan, S.1    Junker, A.2    Helmann, J.D.3    Mascher, T.4
  • 22
    • 37349034233 scopus 로고    scopus 로고
    • Cell envelope stress response in Gram-positive bacteria
    • Jordan, S., Hutchings, M.I., and Mascher, T. (2008) Cell envelope stress response in Gram-positive bacteria. FEMS Microbiol Rev 32: 107-146.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 107-146
    • Jordan, S.1    Hutchings, M.I.2    Mascher, T.3
  • 23
    • 34547614468 scopus 로고    scopus 로고
    • The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators
    • Klein, A.H., Shulla, A., Reimann, S.A., Keating, D.H., and Wolfe, A.J. (2007) The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators. J Bacteriol 189: 5574-5581.
    • (2007) J Bacteriol , vol.189 , pp. 5574-5581
    • Klein, A.H.1    Shulla, A.2    Reimann, S.A.3    Keating, D.H.4    Wolfe, A.J.5
  • 24
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub, M.T., and Goulian, M. (2007) Specificity in two-component signal transduction pathways. Annu Rev Genet 41: 121-145.
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 25
    • 84866368518 scopus 로고    scopus 로고
    • Inhibition of acetyl phosphate-dependent transcription by an acetylatable lysine on RNA polymerase
    • Lima, B.P., Thanh Huyen, T.T., Basell, K., Becher, D., Antelmann, H., and Wolfe, A.J. (2012) Inhibition of acetyl phosphate-dependent transcription by an acetylatable lysine on RNA polymerase. J Biol Chem 287: 32147-32160.
    • (2012) J Biol Chem , vol.287 , pp. 32147-32160
    • Lima, B.P.1    Thanh Huyen, T.T.2    Basell, K.3    Becher, D.4    Antelmann, H.5    Wolfe, A.J.6
  • 26
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary, W., and Stock, J. (1994) Acetyl phosphate and the activation of two-component response regulators. J Biol Chem 269: 31567-31572.
    • (1994) J Biol Chem , vol.269 , pp. 31567-31572
    • McCleary, W.1    Stock, J.2
  • 27
    • 0026721820 scopus 로고
    • Mutagenesis of the Bacillus subtilis '-12, -24' promoter of the levanase operon and evidence for the existence of an upstream activating sequence
    • Martin-Verstraete, I., Debarbouille, M., Klier, A., and Rapoport, G. (1992) Mutagenesis of the Bacillus subtilis '-12, -24' promoter of the levanase operon and evidence for the existence of an upstream activating sequence. J Mol Biol 226: 85-99.
    • (1992) J Mol Biol , vol.226 , pp. 85-99
    • Martin-Verstraete, I.1    Debarbouille, M.2    Klier, A.3    Rapoport, G.4
  • 28
    • 0348147592 scopus 로고    scopus 로고
    • Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon
    • Mascher, T., Margulis, N.G., Wang, T., Ye, R.W., and Helmann, J.D. (2003) Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon. Mol Microbiol 50: 1591-1604.
    • (2003) Mol Microbiol , vol.50 , pp. 1591-1604
    • Mascher, T.1    Margulis, N.G.2    Wang, T.3    Ye, R.W.4    Helmann, J.D.5
  • 29
    • 3342908566 scopus 로고    scopus 로고
    • Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis
    • Mascher, T., Zimmer, S.L., Smith, T.A., and Helmann, J.D. (2004) Antibiotic-inducible promoter regulated by the cell envelope stress-sensing two-component system LiaRS of Bacillus subtilis. Antimicrob Agents Chemother 48: 2888-2896.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2888-2896
    • Mascher, T.1    Zimmer, S.L.2    Smith, T.A.3    Helmann, J.D.4
  • 30
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher, T., Helmann, J.D., and Unden, G. (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 90: 910-938.
    • (2006) Microbiol Mol Biol Rev , vol.90 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 31
  • 32
    • 0030907620 scopus 로고    scopus 로고
    • The Escherichia coli phage-shock-protein (psp) operon
    • Model, P., Jovanovic, G., and Dworkin, J. (1997) The Escherichia coli phage-shock-protein (psp) operon. Mol Microbiol 24: 255-261.
    • (1997) Mol Microbiol , vol.24 , pp. 255-261
    • Model, P.1    Jovanovic, G.2    Dworkin, J.3
  • 33
    • 0020384747 scopus 로고
    • Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis
    • Moran, C.P., Jr, Lang, N., LeGrice, S.F., Lee, G., Stephens, M., Sonenshein, A.L., etal. (1982) Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis. Mol Gen Genet 186: 339-346.
    • (1982) Mol Gen Genet , vol.186 , pp. 339-346
    • Moran Jr., C.P.1    Lang, N.2    LeGrice, S.F.3    Lee, G.4    Stephens, M.5    Sonenshein, A.L.6
  • 34
    • 33748484297 scopus 로고    scopus 로고
    • Co-regulation of motility, exoenzyme and antibiotic production by the EnvZ-OmpR-FlhDC-FliA pathway in Xenorhabdus nematophila
    • Park, D., and Forst, S. (2006) Co-regulation of motility, exoenzyme and antibiotic production by the EnvZ-OmpR-FlhDC-FliA pathway in Xenorhabdus nematophila. Mol Microbiol 61: 1397-1412.
    • (2006) Mol Microbiol , vol.61 , pp. 1397-1412
    • Park, D.1    Forst, S.2
  • 35
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson, J.S. (1993) Signal transduction schemes of bacteria. Cell 73: 857-871.
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 36
    • 19044379164 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides elicit a complex stress response in Bacillus subtilis that involves ECF-type sigma factors and two-component signal transduction systems
    • Pietiäinen, M., Gardemeister, M., Mecklin, M., Leskela, S., Sarvas, M., and Kontinen, V. (2005) Cationic antimicrobial peptides elicit a complex stress response in Bacillus subtilis that involves ECF-type sigma factors and two-component signal transduction systems. Microbiology 151: 1577-1592.
    • (2005) Microbiology , vol.151 , pp. 1577-1592
    • Pietiäinen, M.1    Gardemeister, M.2    Mecklin, M.3    Leskela, S.4    Sarvas, M.5    Kontinen, V.6
  • 37
    • 78649642416 scopus 로고    scopus 로고
    • Instability of ackA (acetate kinase) mutations and their effects on acetyl phosphate and ATP amounts in Streptococcus pneumoniae D39
    • Ramos-Montanez, S., Kazmierczak, K.M., Hentchel, K.L., and Winkler, M.E. (2010) Instability of ackA (acetate kinase) mutations and their effects on acetyl phosphate and ATP amounts in Streptococcus pneumoniae D39. J Bacteriol 192: 6390-6400.
    • (2010) J Bacteriol , vol.192 , pp. 6390-6400
    • Ramos-Montanez, S.1    Kazmierczak, K.M.2    Hentchel, K.L.3    Winkler, M.E.4
  • 38
    • 0027524789 scopus 로고
    • Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • Stülke, J., Hanschke, R., and Hecker, M. (1993) Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool. J Gen Microbiol 139: 2041-2045.
    • (1993) J Gen Microbiol , vol.139 , pp. 2041-2045
    • Stülke, J.1    Hanschke, R.2    Hecker, M.3
  • 39
    • 0030742667 scopus 로고    scopus 로고
    • Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT
    • Stülke, J., Martin-Verstraete, I., Zagorec, M., Rose, M., Klier, A., and Rapoport, G. (1997) Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled by a novel antiterminator, GlcT. Mol Microbiol 25: 65-78.
    • (1997) Mol Microbiol , vol.25 , pp. 65-78
    • Stülke, J.1    Martin-Verstraete, I.2    Zagorec, M.3    Rose, M.4    Klier, A.5    Rapoport, G.6
  • 42
    • 0028021803 scopus 로고
    • Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli
    • Schröder, I., Wolin, C.D., Cavicchioli, R., and Gunsalus, R.P. (1994) Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli. J Bacteriol 176: 4985-4992.
    • (1994) J Bacteriol , vol.176 , pp. 4985-4992
    • Schröder, I.1    Wolin, C.D.2    Cavicchioli, R.3    Gunsalus, R.P.4
  • 44
    • 65549123767 scopus 로고    scopus 로고
    • The LiaFSR system regulates the cell envelope stress response in Streptococcus mutans
    • Suntharalingam, P., Senadheera, M.D., Mair, R.W., Levesque, C.M., and Cvitkovitch, D.G. (2009) The LiaFSR system regulates the cell envelope stress response in Streptococcus mutans. J Bacteriol 191: 2973-2984.
    • (2009) J Bacteriol , vol.191 , pp. 2973-2984
    • Suntharalingam, P.1    Senadheera, M.D.2    Mair, R.W.3    Levesque, C.M.4    Cvitkovitch, D.G.5
  • 46
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach, A. (1996) PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12: 259-265.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 47
    • 77956540008 scopus 로고    scopus 로고
    • Localization and cellular amounts of the WalRKJ (VicRKX) two-component regulatory system proteins in serotype 2 Streptococcus pneumoniae
    • Wayne, K.J., Sham, L.T., Tsui, H.C., Gutu, A.D., Barendt, S.M., Keen, S.K., and Winkler, M.E. (2010) Localization and cellular amounts of the WalRKJ (VicRKX) two-component regulatory system proteins in serotype 2 Streptococcus pneumoniae. J Bacteriol 192: 4388-4394.
    • (2010) J Bacteriol , vol.192 , pp. 4388-4394
    • Wayne, K.J.1    Sham, L.T.2    Tsui, H.C.3    Gutu, A.D.4    Barendt, S.M.5    Keen, S.K.6    Winkler, M.E.7
  • 48
    • 65649091353 scopus 로고    scopus 로고
    • Daptomycin versus friulimicin B: in-depth profiling of Bacillus subtilis cell envelope stress responses
    • Wecke, T., Zühlke, D., Mäder, U., Jordan, S., Voigt, B., Pelzer, S., etal. (2009) Daptomycin versus friulimicin B: in-depth profiling of Bacillus subtilis cell envelope stress responses. Antimicrob Agents Chemother 53: 1619-1623.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1619-1623
    • Wecke, T.1    Zühlke, D.2    Mäder, U.3    Jordan, S.4    Voigt, B.5    Pelzer, S.6
  • 49
    • 0026058969 scopus 로고
    • Sequence and properties of comQ, a new competence regulatory gene of Bacillus subtilis
    • Weinrauch, Y., Msadek, T., Kunst, F., and Dubnau, D. (1991) Sequence and properties of comQ, a new competence regulatory gene of Bacillus subtilis. J Bacteriol 173: 5685-5693.
    • (1991) J Bacteriol , vol.173 , pp. 5685-5693
    • Weinrauch, Y.1    Msadek, T.2    Kunst, F.3    Dubnau, D.4
  • 51
  • 53
    • 77949914858 scopus 로고    scopus 로고
    • Physiologically relevant small phosphodonors link metabolism to signal transduction
    • Wolfe, A.J. (2010) Physiologically relevant small phosphodonors link metabolism to signal transduction. Curr Opin Microbiol 13: 204-209.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 204-209
    • Wolfe, A.J.1
  • 54
    • 41549102957 scopus 로고    scopus 로고
    • Signal integration by the two-component signal transduction response regulator CpxR
    • Wolfe, A.J., Parikh, N., Lima, B., and Zemaitaitis, B. (2008) Signal integration by the two-component signal transduction response regulator CpxR. J Bacteriol 190: 2314-2322.
    • (2008) J Bacteriol , vol.190 , pp. 2314-2322
    • Wolfe, A.J.1    Parikh, N.2    Lima, B.3    Zemaitaitis, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.