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Volumn 11, Issue 6, 2015, Pages

The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; EUKARYOTIC LIKE SERINE THREONINE KINASE PRKC; EUKARYOTIC LIKE SERINE THREONINE PHOSPHATASE PRPC; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PROTEIN SERINE THREONINE KINASE; YYCF PROTEIN, BACTERIA;

EID: 84937782702     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1005275     Document Type: Article
Times cited : (65)

References (65)
  • 1
    • 84862596522 scopus 로고    scopus 로고
    • Impact of phosphoproteomics on studies of bacterial physiology
    • Mijakovic I, Macek B, (2012) Impact of phosphoproteomics on studies of bacterial physiology. FEMS Microbiol Rev 36: 877–892. doi: 10.1111/j.1574-6976.2011.00314.x 22091997
    • (2012) FEMS Microbiol Rev , vol.36 , pp. 877-892
    • Mijakovic, I.1    Macek, B.2
  • 2
    • 84921498354 scopus 로고    scopus 로고
    • Ser/Thr phosphorylation as a regulatory mechanism in bacteria
    • Dworkin J, (2015) Ser/Thr phosphorylation as a regulatory mechanism in bacteria. Curr Opin Microbiol 24C: 47–52.
    • (2015) Curr Opin Microbiol , vol.24C , pp. 47-52
    • Dworkin, J.1
  • 3
  • 4
    • 67649401960 scopus 로고    scopus 로고
    • Transcriptome and functional analysis of the eukaryotic-type ser/thr kinase PknB in Staphylococcus aureus
    • Donat S, Streker K, Schirmeister T, Rakette S, Stehle T, et al. (2009) Transcriptome and functional analysis of the eukaryotic-type ser/thr kinase PknB in Staphylococcus aureus. J Bacteriol 191: 4056–4069. doi: 10.1128/JB.00117-09 19376851
    • (2009) J Bacteriol , vol.191 , pp. 4056-4069
    • Donat, S.1    Streker, K.2    Schirmeister, T.3    Rakette, S.4    Stehle, T.5
  • 5
    • 34249801777 scopus 로고    scopus 로고
    • Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae
    • Saskova L, Novakova L, Basler M, Branny P, (2007) Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae. J Bacteriol 189: 4168–4179. 17416671
    • (2007) J Bacteriol , vol.189 , pp. 4168-4179
    • Saskova, L.1    Novakova, L.2    Basler, M.3    Branny, P.4
  • 6
    • 77951248837 scopus 로고    scopus 로고
    • The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism
    • Banu LD, Conrads G, Rehrauer H, Hussain H, Allan E, et al. (2010) The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism. Infect Immun 78: 2209–2220. doi: 10.1128/IAI.01167-09 20231406
    • (2010) Infect Immun , vol.78 , pp. 2209-2220
    • Banu, L.D.1    Conrads, G.2    Rehrauer, H.3    Hussain, H.4    Allan, E.5
  • 7
    • 84861817863 scopus 로고    scopus 로고
    • Regulation of prokaryotic gene expression by eukaryotic-like enzymes
    • Burnside K, Rajagopal L, (2012) Regulation of prokaryotic gene expression by eukaryotic-like enzymes. Curr Opin Microbiol 15: 125–131. doi: 10.1016/j.mib.2011.12.006 22221896
    • (2012) Curr Opin Microbiol , vol.15 , pp. 125-131
    • Burnside, K.1    Rajagopal, L.2
  • 8
    • 84921933274 scopus 로고    scopus 로고
    • Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens
    • Wright DP, Ulijasz AT, (2014) Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens. Virulence 5: 863–885. doi: 10.4161/21505594.2014.983404 25603430
    • (2014) Virulence , vol.5 , pp. 863-885
    • Wright, D.P.1    Ulijasz, A.T.2
  • 9
    • 33750444279 scopus 로고    scopus 로고
    • Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside
    • Jones G, Dyson P, (2006) Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside. J Bacteriol 188: 7470–7476. 16936012
    • (2006) J Bacteriol , vol.188 , pp. 7470-7476
    • Jones, G.1    Dyson, P.2
  • 10
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: a beta-lactam-binding domain
    • Yeats C, Finn RD, Bateman A, (2002) The PASTA domain: a beta-lactam-binding domain. Trends Biochem Sci 27: 438. 12217513
    • (2002) Trends Biochem Sci , vol.27 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 11
    • 78651376345 scopus 로고    scopus 로고
    • Recognition of peptidoglycan and beta-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae
    • Maestro B, Novakova L, Hesek D, Lee M, Leyva E, et al. (2011) Recognition of peptidoglycan and beta-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae. FEBS Lett 585: 357–363. doi: 10.1016/j.febslet.2010.12.016 21167155
    • (2011) FEBS Lett , vol.585 , pp. 357-363
    • Maestro, B.1    Novakova, L.2    Hesek, D.3    Lee, M.4    Leyva, E.5
  • 12
    • 79960964670 scopus 로고    scopus 로고
    • The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization
    • Mir M, Asong J, Li X, Cardot J, Boons GJ, et al. (2011) The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLoS pathogens 7: e1002182. doi: 10.1371/journal.ppat.1002182 21829358
    • (2011) PLoS pathogens , vol.7 , pp. 1002182
    • Mir, M.1    Asong, J.2    Li, X.3    Cardot, J.4    Boons, G.J.5
  • 13
    • 84555178075 scopus 로고    scopus 로고
    • Chemical Basis of Peptidoglycan Discrimination by PrkC, a Key Kinase Involved in Bacterial Resuscitation from Dormancy
    • Squeglia F, Marchetti R, Ruggiero A, Lanzetta R, Marasco D, et al. (2011) Chemical Basis of Peptidoglycan Discrimination by PrkC, a Key Kinase Involved in Bacterial Resuscitation from Dormancy. Journal of the American Chemical Society 133: 20676–20679. doi: 10.1021/ja208080r 22111897
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 20676-20679
    • Squeglia, F.1    Marchetti, R.2    Ruggiero, A.3    Lanzetta, R.4    Marasco, D.5
  • 14
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah IM, Laaberki MH, Popham DL, Dworkin J, (2008) A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135: 486–496. doi: 10.1016/j.cell.2008.08.039 18984160
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 15
    • 77349111103 scopus 로고    scopus 로고
    • Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides
    • Shah IM, Dworkin J, (2010) Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides. Mol Microbiol 75: 1232–1245. doi: 10.1111/j.1365-2958.2010.07046.x 20070526
    • (2010) Mol Microbiol , vol.75 , pp. 1232-1245
    • Shah, I.M.1    Dworkin, J.2
  • 16
    • 84857683425 scopus 로고    scopus 로고
    • Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis
    • Nicolas P, Mader U, Dervyn E, Rochat T, Leduc A, et al. (2012) Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis. Science 335: 1103–1106. doi: 10.1126/science.1206848 22383849
    • (2012) Science , vol.335 , pp. 1103-1106
    • Nicolas, P.1    Mader, U.2    Dervyn, E.3    Rochat, T.4    Leduc, A.5
  • 17
    • 41949119968 scopus 로고    scopus 로고
    • Essentiality, bypass, and targeting of the YycFG (VicRK) two-component regulatory system in gram-positive bacteria
    • Winkler ME, Hoch JA, (2008) Essentiality, bypass, and targeting of the YycFG (VicRK) two-component regulatory system in gram-positive bacteria. J Bacteriol 190: 2645–2648. doi: 10.1128/JB.01682-07 18245295
    • (2008) J Bacteriol , vol.190 , pp. 2645-2648
    • Winkler, M.E.1    Hoch, J.A.2
  • 18
    • 56749173808 scopus 로고    scopus 로고
    • A matter of life and death: cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway
    • Dubrac S, Bisicchia P, Devine KM, Msadek T, (2008) A matter of life and death: cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway. Mol Microbiol 70: 1307–1322. doi: 10.1111/j.1365-2958.2008.06483.x 19019149
    • (2008) Mol Microbiol , vol.70 , pp. 1307-1322
    • Dubrac, S.1    Bisicchia, P.2    Devine, K.M.3    Msadek, T.4
  • 19
    • 0031757758 scopus 로고    scopus 로고
    • A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy
    • Fabret C, Hoch JA, (1998) A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy. J Bacteriol 180: 6375–6383. 9829949
    • (1998) J Bacteriol , vol.180 , pp. 6375-6383
    • Fabret, C.1    Hoch, J.A.2
  • 20
    • 84155171318 scopus 로고    scopus 로고
    • The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus
    • Dominguez-Cuevas P, Mercier R, Leaver M, Kawai Y, Errington J, (2012) The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus. Molecular microbiology 83: 52–66. doi: 10.1111/j.1365-2958.2011.07920.x 22122227
    • (2012) Molecular microbiology , vol.83 , pp. 52-66
    • Dominguez-Cuevas, P.1    Mercier, R.2    Leaver, M.3    Kawai, Y.4    Errington, J.5
  • 21
    • 0346256788 scopus 로고    scopus 로고
    • Constitutive expression of PcsB suppresses the requirement for the essential VicR (YycF) response regulator in Streptococcus pneumoniae R6
    • Ng WL, Robertson GT, Kazmierczak KM, Zhao J, Gilmour R, et al. (2003) Constitutive expression of PcsB suppresses the requirement for the essential VicR (YycF) response regulator in Streptococcus pneumoniae R6. Molecular microbiology 50: 1647–1663. 14651645
    • (2003) Molecular microbiology , vol.50 , pp. 1647-1663
    • Ng, W.L.1    Robertson, G.T.2    Kazmierczak, K.M.3    Zhao, J.4    Gilmour, R.5
  • 22
    • 0141677726 scopus 로고    scopus 로고
    • Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach
    • Howell A, Dubrac S, Andersen KK, Noone D, Fert J, et al. (2003) Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach. Mol Microbiol 49: 1639–1655. 12950927
    • (2003) Mol Microbiol , vol.49 , pp. 1639-1655
    • Howell, A.1    Dubrac, S.2    Andersen, K.K.3    Noone, D.4    Fert, J.5
  • 23
    • 34250632446 scopus 로고    scopus 로고
    • The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis
    • Bisicchia P, Noone D, Lioliou E, Howell A, Quigley S, et al. (2007) The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis. Mol Microbiol 65: 180–200. 17581128
    • (2007) Mol Microbiol , vol.65 , pp. 180-200
    • Bisicchia, P.1    Noone, D.2    Lioliou, E.3    Howell, A.4    Quigley, S.5
  • 24
    • 36549008206 scopus 로고    scopus 로고
    • New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus
    • Dubrac S, Boneca IG, Poupel O, Msadek T, (2007) New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus. Journal of bacteriology 189: 8257–8269. 17827301
    • (2007) Journal of bacteriology , vol.189 , pp. 8257-8269
    • Dubrac, S.1    Boneca, I.G.2    Poupel, O.3    Msadek, T.4
  • 25
    • 84871457034 scopus 로고    scopus 로고
    • The WalRK (YycFG) and sigma(I) RsgI regulators cooperate to control CwlO and LytE expression in exponentially growing and stressed Bacillus subtilis cells
    • Salzberg LI, Powell L, Hokamp K, Botella E, Noone D, et al. (2013) The WalRK (YycFG) and sigma(I) RsgI regulators cooperate to control CwlO and LytE expression in exponentially growing and stressed Bacillus subtilis cells. Mol Microbiol 87: 180–195. doi: 10.1111/mmi.12092 23199363
    • (2013) Mol Microbiol , vol.87 , pp. 180-195
    • Salzberg, L.I.1    Powell, L.2    Hokamp, K.3    Botella, E.4    Noone, D.5
  • 26
    • 80855141106 scopus 로고    scopus 로고
    • Serine/threonine protein kinase Stk is required for virulence, stress response, and penicillin tolerance in Streptococcus pyogenes
    • Bugrysheva J, Froehlich BJ, Freiberg JA, Scott JR, (2011) Serine/threonine protein kinase Stk is required for virulence, stress response, and penicillin tolerance in Streptococcus pyogenes. Infection and Immunity 79: 4201–4209. doi: 10.1128/IAI.05360-11 21788381
    • (2011) Infection and Immunity , vol.79 , pp. 4201-4209
    • Bugrysheva, J.1    Froehlich, B.J.2    Freiberg, J.A.3    Scott, J.R.4
  • 27
    • 22544460491 scopus 로고    scopus 로고
    • YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis
    • Szurmant H, Nelson K, Kim EJ, Perego M, Hoch JA, (2005) YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis. J Bacteriol 187: 5419–5426. 16030236
    • (2005) J Bacteriol , vol.187 , pp. 5419-5426
    • Szurmant, H.1    Nelson, K.2    Kim, E.J.3    Perego, M.4    Hoch, J.A.5
  • 28
    • 0034773146 scopus 로고    scopus 로고
    • agr expression precedes escape of internalized Staphylococcus aureus from the host endosome
    • Qazi SN, Counil E, Morrissey J, Rees CE, Cockayne A, et al. (2001) agr expression precedes escape of internalized Staphylococcus aureus from the host endosome. Infect Immun 69: 7074–7082. 11598083
    • (2001) Infect Immun , vol.69 , pp. 7074-7082
    • Qazi, S.N.1    Counil, E.2    Morrissey, J.3    Rees, C.E.4    Cockayne, A.5
  • 29
    • 84888599866 scopus 로고    scopus 로고
    • The Bacillus BioBrick Box: generation and evaluation of essential genetic building blocks for standardized work with Bacillus subtilis
    • Radeck J, Kraft K, Bartels J, Cikovic T, Durr F, et al. (2013) The Bacillus BioBrick Box: generation and evaluation of essential genetic building blocks for standardized work with Bacillus subtilis. J Biol Eng 7: 29. doi: 10.1186/1754-1611-7-29 24295448
    • (2013) J Biol Eng , vol.7 , pp. 29
    • Radeck, J.1    Kraft, K.2    Bartels, J.3    Cikovic, T.4    Durr, F.5
  • 30
    • 0036842045 scopus 로고    scopus 로고
    • The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells
    • Gaidenko TA, Kim TJ, Price CW, (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol 184: 6109–6114. 12399479
    • (2002) J Bacteriol , vol.184 , pp. 6109-6114
    • Gaidenko, T.A.1    Kim, T.J.2    Price, C.W.3
  • 31
    • 80052351887 scopus 로고    scopus 로고
    • Cell envelope gene expression in phosphate-limited Bacillus subtilis cells
    • Botella E, Hubner S, Hokamp K, Hansen A, Bisicchia P, et al. (2011) Cell envelope gene expression in phosphate-limited Bacillus subtilis cells. Microbiology 157: 2470–2484. doi: 10.1099/mic.0.049205-0 21636651
    • (2011) Microbiology , vol.157 , pp. 2470-2484
    • Botella, E.1    Hubner, S.2    Hokamp, K.3    Hansen, A.4    Bisicchia, P.5
  • 32
    • 51649118149 scopus 로고    scopus 로고
    • Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis
    • Yamamoto H, Hashimoto M, Higashitsuji Y, Harada H, Hariyama N, et al. (2008) Post-translational control of vegetative cell separation enzymes through a direct interaction with specific inhibitor IseA in Bacillus subtilis. Mol Microbiol 70: 168–182. doi: 10.1111/j.1365-2958.2008.06398.x 18761694
    • (2008) Mol Microbiol , vol.70 , pp. 168-182
    • Yamamoto, H.1    Hashimoto, M.2    Higashitsuji, Y.3    Harada, H.4    Hariyama, N.5
  • 33
    • 84858952375 scopus 로고    scopus 로고
    • Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis
    • Kobayashi K, Sudiarta IP, Kodama T, Fukushima T, Ara K, et al. (2012) Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis. J Biol Chem 287: 9765–9776. doi: 10.1074/jbc.M111.329490 22277649
    • (2012) J Biol Chem , vol.287 , pp. 9765-9776
    • Kobayashi, K.1    Sudiarta, I.P.2    Kodama, T.3    Fukushima, T.4    Ara, K.5
  • 34
    • 0038047139 scopus 로고    scopus 로고
    • Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis
    • Madec E, Stensballe A, Kjellstrom S, Cladiere L, Obuchowski M, et al. (2003) Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis. J Mol Biol 330: 459–472. 12842463
    • (2003) J Mol Biol , vol.330 , pp. 459-472
    • Madec, E.1    Stensballe, A.2    Kjellstrom, S.3    Cladiere, L.4    Obuchowski, M.5
  • 35
    • 77952132933 scopus 로고    scopus 로고
    • Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases
    • Prisic S, Dankwa S, Schwartz D, Chou MF, Locasale JW, et al. (2010) Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases. Proc Natl Acad Sci U S A 107: 7521–7526. doi: 10.1073/pnas.0913482107 20368441
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7521-7526
    • Prisic, S.1    Dankwa, S.2    Schwartz, D.3    Chou, M.F.4    Locasale, J.W.5
  • 36
    • 46949100415 scopus 로고    scopus 로고
    • A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis
    • Fukushima T, Szurmant H, Kim EJ, Perego M, Hoch JA, (2008) A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis. Molecular microbiology 69: 621–632. doi: 10.1111/j.1365-2958.2008.06308.x 18573169
    • (2008) Molecular microbiology , vol.69 , pp. 621-632
    • Fukushima, T.1    Szurmant, H.2    Kim, E.J.3    Perego, M.4    Hoch, J.A.5
  • 37
    • 78651103071 scopus 로고    scopus 로고
    • A role for the essential YycG sensor histidine kinase in sensing cell division
    • Fukushima T, Furihata I, Emmins R, Daniel RA, Hoch JA, et al. (2011) A role for the essential YycG sensor histidine kinase in sensing cell division. Mol Microbiol 79: 503–522. doi: 10.1111/j.1365-2958.2010.07464.x 21219466
    • (2011) Mol Microbiol , vol.79 , pp. 503-522
    • Fukushima, T.1    Furihata, I.2    Emmins, R.3    Daniel, R.A.4    Hoch, J.A.5
  • 38
    • 34247849321 scopus 로고    scopus 로고
    • YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis
    • Szurmant H, Mohan MA, Imus PM, Hoch JA, (2007) YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. J Bacteriol 189: 3280–3289. 17307850
    • (2007) J Bacteriol , vol.189 , pp. 3280-3289
    • Szurmant, H.1    Mohan, M.A.2    Imus, P.M.3    Hoch, J.A.4
  • 39
    • 44449149782 scopus 로고    scopus 로고
    • An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins
    • Szurmant H, Bu L, Brooks CL, 3rdHoch JA, (2008) An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins. Proc Natl Acad Sci U S A 105: 5891–5896. doi: 10.1073/pnas.0800247105 18408157
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5891-5896
    • Szurmant, H.1    Bu, L.2    Brooks, C.L.3    Hoch, J.A.4
  • 40
    • 18144411635 scopus 로고    scopus 로고
    • Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face
    • Toro-Roman A, Mack TR, Stock AM, (2005) Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face. J Mol Biol 349: 11–26. 15876365
    • (2005) J Mol Biol , vol.349 , pp. 11-26
    • Toro-Roman, A.1    Mack, T.R.2    Stock, A.M.3
  • 41
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • Bourret RB, (2010) Receiver domain structure and function in response regulator proteins. Curr Opin Microbiol 13: 142–149. doi: 10.1016/j.mib.2010.01.015 20211578
    • (2010) Curr Opin Microbiol , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 42
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern D, Volkman BF, Luginbuhl P, Nohaile MJ, Kustu S, et al. (1999) Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 402: 894–898. 10622255
    • (1999) Nature , vol.402 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.J.4    Kustu, S.5
  • 43
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P, Rubio V, Marina A, (2009) Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139: 325–336. doi: 10.1016/j.cell.2009.08.032 19800110
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 44
    • 78649704332 scopus 로고    scopus 로고
    • Systematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways
    • Capra EJ, Perchuk BS, Lubin EA, Ashenberg O, Skerker JM, et al. (2010) Systematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways. PLoS Genet 6: e1001220. doi: 10.1371/journal.pgen.1001220 21124821
    • (2010) PLoS Genet , vol.6 , pp. 1001220
    • Capra, E.J.1    Perchuk, B.S.2    Lubin, E.A.3    Ashenberg, O.4    Skerker, J.M.5
  • 45
    • 64049118984 scopus 로고    scopus 로고
    • CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis
    • Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, et al. (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155: 932–943. doi: 10.1099/mic.0.022475-0 19246764
    • (2009) Microbiology , vol.155 , pp. 932-943
    • Absalon, C.1    Obuchowski, M.2    Madec, E.3    Delattre, D.4    Holland, I.B.5
  • 46
    • 84862288122 scopus 로고    scopus 로고
    • Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology
    • Pompeo F, Freton C, Wicker-Planquart C, Grangeasse C, Jault JM, et al. (2012) Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology. J Biol Chem 287: 20830–20838. doi: 10.1074/jbc.M112.340331 22544754
    • (2012) J Biol Chem , vol.287 , pp. 20830-20838
    • Pompeo, F.1    Freton, C.2    Wicker-Planquart, C.3    Grangeasse, C.4    Jault, J.M.5
  • 47
    • 84905281353 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC
    • Ravikumar V, Shi L, Krug K, Derouiche A, Jers C, et al. (2014) Quantitative phosphoproteome analysis of bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC. Mol Cell Proteomics 13: 1965–1978. doi: 10.1074/mcp.M113.035949 24390483
    • (2014) Mol Cell Proteomics , vol.13 , pp. 1965-1978
    • Ravikumar, V.1    Shi, L.2    Krug, K.3    Derouiche, A.4    Jers, C.5
  • 48
    • 84906536742 scopus 로고    scopus 로고
    • PrkC-mediated Phosphorylation of Overexpressed YvcK Protein Regulates PBP1 Protein Localization in Bacillus subtilis mreB Mutant Cells
    • Foulquier E, Pompeo F, Freton C, Cordier B, Grangeasse C, et al. (2014) PrkC-mediated Phosphorylation of Overexpressed YvcK Protein Regulates PBP1 Protein Localization in Bacillus subtilis mreB Mutant Cells. J Biol Chem 289: 23662–23669. doi: 10.1074/jbc.M114.562496 25012659
    • (2014) J Biol Chem , vol.289 , pp. 23662-23669
    • Foulquier, E.1    Pompeo, F.2    Freton, C.3    Cordier, B.4    Grangeasse, C.5
  • 49
    • 77950616042 scopus 로고    scopus 로고
    • In vitro Phosphorylation of Key Metabolic Enzymes from Bacillus subtilis: PrkC Phosphorylates Enzymes from Different Branches of Basic Metabolism
    • Pietack N, Becher D, Schmidl SR, Saier MH, Hecker M, et al. (2010) In vitro Phosphorylation of Key Metabolic Enzymes from Bacillus subtilis: PrkC Phosphorylates Enzymes from Different Branches of Basic Metabolism. J Mol Microbiol Biotechnol 18: 129–140. doi: 10.1159/000308512 20389117
    • (2010) J Mol Microbiol Biotechnol , vol.18 , pp. 129-140
    • Pietack, N.1    Becher, D.2    Schmidl, S.R.3    Saier, M.H.4    Hecker, M.5
  • 50
    • 84901404149 scopus 로고    scopus 로고
    • Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties
    • Kobir A, Poncet S, Bidnenko V, Delumeau O, Jers C, et al. (2014) Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties. Mol Microbiol 92: 1129–1141. doi: 10.1111/mmi.12617 24731262
    • (2014) Mol Microbiol , vol.92 , pp. 1129-1141
    • Kobir, A.1    Poncet, S.2    Bidnenko, V.3    Delumeau, O.4    Jers, C.5
  • 51
    • 84860820090 scopus 로고    scopus 로고
    • Strain-specific regulatory role of eukaryote-like serine/threonine phosphatase in pneumococcal adherence
    • Agarwal S, Agarwal S, Pancholi P, Pancholi V, (2012) Strain-specific regulatory role of eukaryote-like serine/threonine phosphatase in pneumococcal adherence. Infect Immun 80: 1361–1372. doi: 10.1128/IAI.06311-11 22311926
    • (2012) Infect Immun , vol.80 , pp. 1361-1372
    • Agarwal, S.1    Agarwal, S.2    Pancholi, P.3    Pancholi, V.4
  • 52
    • 84901682973 scopus 로고    scopus 로고
    • Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis
    • Horstmann N, Saldana M, Sahasrabhojane P, Yao H, Su X, et al. (2014) Dual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesis. PLoS Pathog 10: e1004088. doi: 10.1371/journal.ppat.1004088 24788524
    • (2014) PLoS Pathog , vol.10 , pp. 1004088
    • Horstmann, N.1    Saldana, M.2    Sahasrabhojane, P.3    Yao, H.4    Su, X.5
  • 53
    • 84887605559 scopus 로고    scopus 로고
    • Two unique phosphorylation-driven signaling pathways crosstalk in Staphylococcus aureus to modulate the cell-wall charge: Stk1/Stp1 meets GraSR
    • Fridman M, Williams GD, Muzamal U, Hunter H, Siu KW, et al. (2013) Two unique phosphorylation-driven signaling pathways crosstalk in Staphylococcus aureus to modulate the cell-wall charge: Stk1/Stp1 meets GraSR. Biochemistry 52: 7975–7986. doi: 10.1021/bi401177n 24102310
    • (2013) Biochemistry , vol.52 , pp. 7975-7986
    • Fridman, M.1    Williams, G.D.2    Muzamal, U.3    Hunter, H.4    Siu, K.W.5
  • 54
    • 84899483277 scopus 로고    scopus 로고
    • A novel mode of regulation of the Staphylococcus aureus Vancomycin-resistance-associated response regulator VraR mediated by Stk1 protein phosphorylation
    • Canova MJ, Baronian G, Brelle S, Cohen-Gonsaud M, Bischoff M, et al. (2014) A novel mode of regulation of the Staphylococcus aureus Vancomycin-resistance-associated response regulator VraR mediated by Stk1 protein phosphorylation. Biochem Biophys Res Commun 447: 165–171. doi: 10.1016/j.bbrc.2014.03.128 24704444
    • (2014) Biochem Biophys Res Commun , vol.447 , pp. 165-171
    • Canova, M.J.1    Baronian, G.2    Brelle, S.3    Cohen-Gonsaud, M.4    Bischoff, M.5
  • 55
    • 77956519362 scopus 로고    scopus 로고
    • Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis
    • Chao JD, Papavinasasundaram KG, Zheng X, Chavez-Steenbock A, Wang X, et al. (2010) Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J Biol Chem 285: 29239–29246. doi: 10.1074/jbc.M110.132894 20630871
    • (2010) J Biol Chem , vol.285 , pp. 29239-29246
    • Chao, J.D.1    Papavinasasundaram, K.G.2    Zheng, X.3    Chavez-Steenbock, A.4    Wang, X.5
  • 56
    • 39149123853 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c
    • Canova MJ, Veyron-Churlet R, Zanella-Cleon I, Cohen-Gonsaud M, Cozzone AJ, et al. (2008) The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c. Proteomics 8: 521–533. doi: 10.1002/pmic.200700442 18175374
    • (2008) Proteomics , vol.8 , pp. 521-533
    • Canova, M.J.1    Veyron-Churlet, R.2    Zanella-Cleon, I.3    Cohen-Gonsaud, M.4    Cozzone, A.J.5
  • 57
    • 67749099836 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation
    • Cohen-Gonsaud M, Barthe P, Canova MJ, Stagier-Simon C, Kremer L, et al. (2009) The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation. J Biol Chem 284: 19290–19300. doi: 10.1074/jbc.M109.019653 19457863
    • (2009) J Biol Chem , vol.284 , pp. 19290-19300
    • Cohen-Gonsaud, M.1    Barthe, P.2    Canova, M.J.3    Stagier-Simon, C.4    Kremer, L.5
  • 58
    • 58149302498 scopus 로고    scopus 로고
    • Phosphorylation of the RitR DNA-binding domain by a Ser-Thr phosphokinase: implications for global gene regulation in the streptococci
    • Ulijasz AT, Falk SP, Weisblum B, (2009) Phosphorylation of the RitR DNA-binding domain by a Ser-Thr phosphokinase: implications for global gene regulation in the streptococci. Mol Microbiol 71: 382–390. doi: 10.1111/j.1365-2958.2008.06532.x 19040630
    • (2009) Mol Microbiol , vol.71 , pp. 382-390
    • Ulijasz, A.T.1    Falk, S.P.2    Weisblum, B.3
  • 59
    • 62449179440 scopus 로고    scopus 로고
    • Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR
    • Lin WJ, Walthers D, Connelly JE, Burnside K, Jewell KA, et al. (2009) Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR. Molecular microbiology 71: 1477–1495. doi: 10.1111/j.1365-2958.2009.06616.x 19170889
    • (2009) Molecular microbiology , vol.71 , pp. 1477-1495
    • Lin, W.J.1    Walthers, D.2    Connelly, J.E.3    Burnside, K.4    Jewell, K.A.5
  • 60
    • 84867594031 scopus 로고    scopus 로고
    • The WalKR system controls major staphylococcal virulence genes and is involved in triggering the host inflammatory response
    • Delaune A, Dubrac S, Blanchet C, Poupel O, Mader U, et al. (2012) The WalKR system controls major staphylococcal virulence genes and is involved in triggering the host inflammatory response. Infect Immun 80: 3438–3453. doi: 10.1128/IAI.00195-12 22825451
    • (2012) Infect Immun , vol.80 , pp. 3438-3453
    • Delaune, A.1    Dubrac, S.2    Blanchet, C.3    Poupel, O.4    Mader, U.5
  • 61
    • 33744485823 scopus 로고    scopus 로고
    • Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus
    • Friedman L, Alder JD, Silverman JA, (2006) Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus. Antimicrob Agents Chemother 50: 2137–2145. 16723576
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2137-2145
    • Friedman, L.1    Alder, J.D.2    Silverman, J.A.3
  • 62
    • 34249674005 scopus 로고    scopus 로고
    • Role of insertion elements and yycFG in the development of decreased susceptibility to vancomycin in Staphylococcus aureus
    • Jansen A, Turck M, Szekat C, Nagel M, Clever I, et al. (2007) Role of insertion elements and yycFG in the development of decreased susceptibility to vancomycin in Staphylococcus aureus. Int J Med Microbiol 297: 205–215. 17418637
    • (2007) Int J Med Microbiol , vol.297 , pp. 205-215
    • Jansen, A.1    Turck, M.2    Szekat, C.3    Nagel, M.4    Clever, I.5
  • 63
    • 81755177765 scopus 로고    scopus 로고
    • Evolution of multidrug resistance during Staphylococcus aureus infection involves mutation of the essential two component regulator WalKR
    • Howden BP, McEvoy CR, Allen DL, Chua K, Gao W, et al. (2011) Evolution of multidrug resistance during Staphylococcus aureus infection involves mutation of the essential two component regulator WalKR. PLoS Pathog 7: e1002359. doi: 10.1371/journal.ppat.1002359 22102812
    • (2011) PLoS Pathog , vol.7 , pp. 1002359
    • Howden, B.P.1    McEvoy, C.R.2    Allen, D.L.3    Chua, K.4    Gao, W.5
  • 64
    • 84868017750 scopus 로고    scopus 로고
    • Contribution of selected gene mutations to resistance in clinical isolates of vancomycin-intermediate Staphylococcus aureus
    • Hafer C, Lin Y, Kornblum J, Lowy FD, Uhlemann AC, (2012) Contribution of selected gene mutations to resistance in clinical isolates of vancomycin-intermediate Staphylococcus aureus. Antimicrob Agents Chemother 56: 5845–5851. doi: 10.1128/AAC.01139-12 22948864
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5845-5851
    • Hafer, C.1    Lin, Y.2    Kornblum, J.3    Lowy, F.D.4    Uhlemann, A.C.5


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