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Volumn 16, Issue 2, 2014, Pages 359-381

The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); CYANOBACTERIA; LEGIONELLA PNEUMOPHILA; PROTOZOA;

EID: 84892958675     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.12223     Document Type: Article
Times cited : (25)

References (90)
  • 1
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • Abascal, F., Zardoya, R., and Posada, D. (2005) ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21: 2014-2015.
    • (2005) Bioinformatics , vol.21 , pp. 2014-2015
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 3
    • 84870687262 scopus 로고    scopus 로고
    • Aquaporin AqpZ is involved in cell volume regulation and sensitivity to osmotic stress in Synechocystis sp. strain PCC 6803
    • Akai, M., Onai, K., Morishita, M., Mino, H., Shijuku, T., Maruyama, H., etal. (2012) Aquaporin AqpZ is involved in cell volume regulation and sensitivity to osmotic stress in Synechocystis sp. strain PCC 6803. J Bacteriol 194: 6828-6836.
    • (2012) J Bacteriol , vol.194 , pp. 6828-6836
    • Akai, M.1    Onai, K.2    Morishita, M.3    Mino, H.4    Shijuku, T.5    Maruyama, H.6
  • 4
    • 40849145295 scopus 로고    scopus 로고
    • Assembly and disassembly dynamics of the cyanobacterial periodosome
    • Akiyama, S., Nohara, A., Ito, K., and Maéda, Y. (2008) Assembly and disassembly dynamics of the cyanobacterial periodosome. Mol Cell 29: 703-716.
    • (2008) Mol Cell , vol.29 , pp. 703-716
    • Akiyama, S.1    Nohara, A.2    Ito, K.3    Maéda, Y.4
  • 5
    • 73649119529 scopus 로고    scopus 로고
    • Control of flagellar gene regulation in Legionella pneumophila and its relation to growth phase
    • Albert-Weissenberger, C., Sahr, T., Sismeiro, O., Hacker, J., Heuner, K., and Buchrieser, C. (2010) Control of flagellar gene regulation in Legionella pneumophila and its relation to growth phase. J Bacteriol 192: 446-455.
    • (2010) J Bacteriol , vol.192 , pp. 446-455
    • Albert-Weissenberger, C.1    Sahr, T.2    Sismeiro, O.3    Hacker, J.4    Heuner, K.5    Buchrieser, C.6
  • 6
    • 40449126813 scopus 로고    scopus 로고
    • The response regulator CpxR directly regulates expression of several Legionella pneumophila icm/dot components as well as new translocated substrates
    • Altman, E., and Segal, G. (2008) The response regulator CpxR directly regulates expression of several Legionella pneumophila icm/dot components as well as new translocated substrates. J Bacteriol 90: 1985-1996.
    • (2008) J Bacteriol , vol.90 , pp. 1985-1996
    • Altman, E.1    Segal, G.2
  • 7
    • 0034968828 scopus 로고    scopus 로고
    • RpoS co-operates with other factors to induce Legionella pneumophila virulence in the stationary phase
    • Bachman, M.A., and Swanson, M.S. (2001) RpoS co-operates with other factors to induce Legionella pneumophila virulence in the stationary phase. Mol Microbiol 40: 1201-1214.
    • (2001) Mol Microbiol , vol.40 , pp. 1201-1214
    • Bachman, M.A.1    Swanson, M.S.2
  • 8
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
    • Baker, L.M., Raudonikiene, A., Hoffman, P.S., and Poole, L.B. (2001) Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J Bacteriol 183: 1961-1973.
    • (2001) J Bacteriol , vol.183 , pp. 1961-1973
    • Baker, L.M.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 9
    • 0034462749 scopus 로고    scopus 로고
    • Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function
    • Bandyopadhyay, P., and Steinman, H.M. (2000) Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function. J Bacteriol 182: 6679-6686.
    • (2000) J Bacteriol , vol.182 , pp. 6679-6686
    • Bandyopadhyay, P.1    Steinman, H.M.2
  • 10
    • 0041764462 scopus 로고    scopus 로고
    • Legionella pneumophila catalase-peroxidases are required for proper trafficking and growth in primary macrophages
    • Bandyopadhyay, P., Byrne, B., Chan, Y., Swanson, M.S., and Steinman, H.M. (2003) Legionella pneumophila catalase-peroxidases are required for proper trafficking and growth in primary macrophages. Infect Immun 71: 4526-4535.
    • (2003) Infect Immun , vol.71 , pp. 4526-4535
    • Bandyopadhyay, P.1    Byrne, B.2    Chan, Y.3    Swanson, M.S.4    Steinman, H.M.5
  • 11
    • 33745767998 scopus 로고    scopus 로고
    • Virulence strategies for infecting phagocytes deduced from the in vivo transcriptional program of Legionella pneumophila
    • Bruggemann, H., Hagman, A., Jules, M., Sismeiro, O., Dillies, M.A., Gouyette, C., etal. (2006) Virulence strategies for infecting phagocytes deduced from the in vivo transcriptional program of Legionella pneumophila. Cell Microbiol 8: 1228-1240.
    • (2006) Cell Microbiol , vol.8 , pp. 1228-1240
    • Bruggemann, H.1    Hagman, A.2    Jules, M.3    Sismeiro, O.4    Dillies, M.A.5    Gouyette, C.6
  • 12
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk, R., Lima, C.D., Erdjument-Bromage, H., Tempst, P., and Nathan, C. (2002) Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 295: 1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 13
    • 0031841662 scopus 로고    scopus 로고
    • Expression of Legionella pneumophila virulence traits in response to growth conditions
    • Byrne, B., and Swanson, M.S. (1998) Expression of Legionella pneumophila virulence traits in response to growth conditions. Infect Immun 66: 3029-3034.
    • (1998) Infect Immun , vol.66 , pp. 3029-3034
    • Byrne, B.1    Swanson, M.S.2
  • 15
    • 0024384046 scopus 로고
    • Characterization of selective inhibition of growth of virulent Legionella pneumophila by supplemented Mueller-Hinton medium
    • Catrenich, C.E., and Johnson, W. (1989) Characterization of selective inhibition of growth of virulent Legionella pneumophila by supplemented Mueller-Hinton medium. Infect Immun 57: 1862-1864.
    • (1989) Infect Immun , vol.57 , pp. 1862-1864
    • Catrenich, C.E.1    Johnson, W.2
  • 16
    • 10044263696 scopus 로고    scopus 로고
    • Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity
    • Cazalet, C., Rusniok, C., Bruggemann, H., Zidane, N., Magnier, A., Ma, L., etal. (2004) Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity. Nat Genet 36: 1165-1173.
    • (2004) Nat Genet , vol.36 , pp. 1165-1173
    • Cazalet, C.1    Rusniok, C.2    Bruggemann, H.3    Zidane, N.4    Magnier, A.5    Ma, L.6
  • 17
    • 77649198508 scopus 로고    scopus 로고
    • Analysis of the Legionella longbeachae genome and transcriptome uncovers unique strategies to cause Legionnaires' disease
    • Cazalet, C., Gomez-Valero, L., Rusniok, C., Lomma, M., Dervins-Ravault, D., Newton, H.J., etal. (2010) Analysis of the Legionella longbeachae genome and transcriptome uncovers unique strategies to cause Legionnaires' disease. PLoS Genet 6: e1000851.
    • (2010) PLoS Genet , vol.6
    • Cazalet, C.1    Gomez-Valero, L.2    Rusniok, C.3    Lomma, M.4    Dervins-Ravault, D.5    Newton, H.J.6
  • 18
    • 84874731065 scopus 로고    scopus 로고
    • Photocycle of the LOV-STAS protein from the pathogen Listeria monocytogenes
    • Chan, R.H., Lewis, J.W., and Bogomolni, R.A. (2013) Photocycle of the LOV-STAS protein from the pathogen Listeria monocytogenes. Photochem Photobiol 89: 361-369.
    • (2013) Photochem Photobiol , vol.89 , pp. 361-369
    • Chan, R.H.1    Lewis, J.W.2    Bogomolni, R.A.3
  • 20
    • 34248666720 scopus 로고    scopus 로고
    • Iron acquisition by Legionella pneumophila
    • Cianciotto, N. (2007) Iron acquisition by Legionella pneumophila. Biometals 20: 323-331.
    • (2007) Biometals , vol.20 , pp. 323-331
    • Cianciotto, N.1
  • 21
    • 77950211392 scopus 로고    scopus 로고
    • Distinct roles of ppGpp and DksA in Legionella pneumophila differentiation
    • Dalebroux, Z.D., Yagi, B.F., Sahr, T., Buchrieser, C., and Swanson, M.S. (2010) Distinct roles of ppGpp and DksA in Legionella pneumophila differentiation. Mol Microbiol 76: 200-219.
    • (2010) Mol Microbiol , vol.76 , pp. 200-219
    • Dalebroux, Z.D.1    Yagi, B.F.2    Sahr, T.3    Buchrieser, C.4    Swanson, M.S.5
  • 22
    • 76749111535 scopus 로고    scopus 로고
    • Elevated ATPase activity of KaiC applies a circadian checkpoint on cell division in Synechococcus elongatus
    • Dong, G., Yang, Q., Wang, Q., Kim, Y.I., Wood, T.L., Osteryoung, K.W., etal. (2010) Elevated ATPase activity of KaiC applies a circadian checkpoint on cell division in Synechococcus elongatus. Cell 140: 529-539.
    • (2010) Cell , vol.140 , pp. 529-539
    • Dong, G.1    Yang, Q.2    Wang, Q.3    Kim, Y.I.4    Wood, T.L.5    Osteryoung, K.W.6
  • 23
    • 0033060648 scopus 로고    scopus 로고
    • On the binding of ATP to the autophosphorylating protein, Ptk, of the bacterium Acinetobacter johnsonii
    • Doublet, P., Vincent, C., Grangeasse, C., Cozzone, A.J., and Duclos, B. (1999) On the binding of ATP to the autophosphorylating protein, Ptk, of the bacterium Acinetobacter johnsonii. FEBS Lett 445: 137-143.
    • (1999) FEBS Lett , vol.445 , pp. 137-143
    • Doublet, P.1    Vincent, C.2    Grangeasse, C.3    Cozzone, A.J.4    Duclos, B.5
  • 24
    • 0344321891 scopus 로고    scopus 로고
    • Origin and evolution of circadian clock genes in prokaryotes
    • Dvornyk, V., Vinogradova, O., and Nevo, E. (2003) Origin and evolution of circadian clock genes in prokaryotes. Proc Natl Acad Sci USA 100: 2495-2500.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2495-2500
    • Dvornyk, V.1    Vinogradova, O.2    Nevo, E.3
  • 25
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 26
    • 84858001166 scopus 로고    scopus 로고
    • Legionella pneumophila transcriptome during intracellular multiplication in human macrophages
    • Faucher, S.P., Mueller, C.A., and Shuman, H.A. (2011) Legionella pneumophila transcriptome during intracellular multiplication in human macrophages. Front Microbiol 2: 60.
    • (2011) Front Microbiol , vol.2 , pp. 60
    • Faucher, S.P.1    Mueller, C.A.2    Shuman, H.A.3
  • 27
    • 0036314980 scopus 로고    scopus 로고
    • Legionella and Legionnaires' disease: 25 years of investigation
    • Fields, B.S., Benson, R.F., and Besser, R.E. (2002) Legionella and Legionnaires' disease: 25 years of investigation. Clin Microbiol Rev 15: 506-526.
    • (2002) Clin Microbiol Rev , vol.15 , pp. 506-526
    • Fields, B.S.1    Benson, R.F.2    Besser, R.E.3
  • 29
    • 81255205278 scopus 로고    scopus 로고
    • Extensive recombination events and horizontal gene transfer shaped the Legionella pneumophila genomes
    • Gomez-Valero, L., Rusniok, C., Jarraud, S., Vacherie, B., Rouy, Z., Barbe, V., etal. (2011) Extensive recombination events and horizontal gene transfer shaped the Legionella pneumophila genomes. BMC Genomics 12: 536.
    • (2011) BMC Genomics , vol.12 , pp. 536
    • Gomez-Valero, L.1    Rusniok, C.2    Jarraud, S.3    Vacherie, B.4    Rouy, Z.5    Barbe, V.6
  • 31
    • 23144433822 scopus 로고    scopus 로고
    • PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference
    • Guindon, S., Lethiec, F., Duroux, P., and Gascuel, O. (2005) PHYML Online - a web server for fast maximum likelihood-based phylogenetic inference. Nucleic Acids Res 33: W557-W559.
    • (2005) Nucleic Acids Res , vol.33
    • Guindon, S.1    Lethiec, F.2    Duroux, P.3    Gascuel, O.4
  • 32
    • 84876820077 scopus 로고    scopus 로고
    • Two antagonistic clock-regulated histidine kinases time the activation of circadian gene expression
    • Gutu, A., and O'Shea, E.K. (2013) Two antagonistic clock-regulated histidine kinases time the activation of circadian gene expression. Mol Cell 50: 288-294.
    • (2013) Mol Cell , vol.50 , pp. 288-294
    • Gutu, A.1    O'Shea, E.K.2
  • 33
    • 0036225745 scopus 로고    scopus 로고
    • A two-component regulator induces the transmission phenotype of stationary-phase Legionella pneumophila
    • Hammer, B.K., Tateda, E.S., and Swanson, M.S. (2002) A two-component regulator induces the transmission phenotype of stationary-phase Legionella pneumophila. Mol Microbiol 44: 107-118.
    • (2002) Mol Microbiol , vol.44 , pp. 107-118
    • Hammer, B.K.1    Tateda, E.S.2    Swanson, M.S.3
  • 34
    • 12844260889 scopus 로고    scopus 로고
    • Role of the stress sigma factor RpoS in GacA/RsmA-controlled secondary metabolism and resistance to oxidative stress in Pseudomonas fluorescens CHA0
    • Heeb, S., Valverde, C., Gigot-Bonnefoy, C., and Haas, D. (2005) Role of the stress sigma factor RpoS in GacA/RsmA-controlled secondary metabolism and resistance to oxidative stress in Pseudomonas fluorescens CHA0. FEMS Microbiol Lett 243: 251-258.
    • (2005) FEMS Microbiol Lett , vol.243 , pp. 251-258
    • Heeb, S.1    Valverde, C.2    Gigot-Bonnefoy, C.3    Haas, D.4
  • 35
    • 80052968825 scopus 로고    scopus 로고
    • Function, structure and mechanism of bacterial photosensory LOV proteins
    • Herrou, J., and Crosson, S. (2011) Function, structure and mechanism of bacterial photosensory LOV proteins. Nat Rev Microbiol 9: 713-723.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 713-723
    • Herrou, J.1    Crosson, S.2
  • 36
    • 0031032030 scopus 로고    scopus 로고
    • An iron- and fur-repressed Legionella pneumophila gene that promotes intracellular infection and encodes a protein with similarity to the Escherichia coli aerobactin synthetases
    • Hickey, E.K., and Cianciotto, N. (1997) An iron- and fur-repressed Legionella pneumophila gene that promotes intracellular infection and encodes a protein with similarity to the Escherichia coli aerobactin synthetases. Infect Immun 65: 133-143.
    • (1997) Infect Immun , vol.65 , pp. 133-143
    • Hickey, E.K.1    Cianciotto, N.2
  • 37
    • 38849137205 scopus 로고    scopus 로고
    • Transcriptional profiling of Legionella pneumophila biofilm cells and the influence of iron on biofilm formation
    • Hindre, T., Bruggemann, H., Buchrieser, C., and Hechard, Y. (2008) Transcriptional profiling of Legionella pneumophila biofilm cells and the influence of iron on biofilm formation. Microbiology 154: 30-41.
    • (2008) Microbiology , vol.154 , pp. 30-41
    • Hindre, T.1    Bruggemann, H.2    Buchrieser, C.3    Hechard, Y.4
  • 38
    • 21444458211 scopus 로고    scopus 로고
    • Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm
    • Hitomi, K., Oyama, T., Han, S., and G. E. Arvai, A.S. (2005) Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm. J Biol Chem 280: 19127-19135.
    • (2005) J Biol Chem , vol.280 , pp. 19127-19135
    • Hitomi, K.1    Oyama, T.2    Han, S.3    Arvai, A.S.G.E.4
  • 39
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • (Web Server Issue)
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: (Web Server Issue): W545-W549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 40
    • 0033104504 scopus 로고    scopus 로고
    • Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria
    • Iwasaki, H., Taniguchi, Y., Ishiura, M., and Kondo, T. (1999) Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria. EMBO J 18: 1137-1145.
    • (1999) EMBO J , vol.18 , pp. 1137-1145
    • Iwasaki, H.1    Taniguchi, Y.2    Ishiura, M.3    Kondo, T.4
  • 41
    • 30044441280 scopus 로고    scopus 로고
    • Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex
    • Iwase, R., Imada, K., Hayashi, F., Uzumaki, T., Morishita, M., Onai, K., etal. (2005) Functionally important substructures of circadian clock protein KaiB in a unique tetramer complex. J Biol Chem 280: 43141-43149.
    • (2005) J Biol Chem , vol.280 , pp. 43141-43149
    • Iwase, R.1    Imada, K.2    Hayashi, F.3    Uzumaki, T.4    Morishita, M.5    Onai, K.6
  • 43
    • 80053033696 scopus 로고    scopus 로고
    • Blue flickers of hope: secondary structure, dynamics, and putative dimerization interface of the blue-light receptor YtvA from Bacillus subtilis
    • Jurk, M., Dorn, M., and Schmieder, P. (2011) Blue flickers of hope: secondary structure, dynamics, and putative dimerization interface of the blue-light receptor YtvA from Bacillus subtilis. Biochemistry 50: 8163-8171.
    • (2011) Biochemistry , vol.50 , pp. 8163-8171
    • Jurk, M.1    Dorn, M.2    Schmieder, P.3
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 45
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA 95: 5752-5756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 46
    • 84873191125 scopus 로고    scopus 로고
    • The Legionella pneumophila orphan sensor kinase LqsT regulates competence and pathogen-host interactions as a component of the LAI-1 circuit
    • Kessler, A., Schell, U., Sahr, T., Tiaden, A., Harrison, C., Buchrieser, C., and Hilbi, H. (2013) The Legionella pneumophila orphan sensor kinase LqsT regulates competence and pathogen-host interactions as a component of the LAI-1 circuit. Environ Microbiol 15: 646-662.
    • (2013) Environ Microbiol , vol.15 , pp. 646-662
    • Kessler, A.1    Schell, U.2    Sahr, T.3    Tiaden, A.4    Harrison, C.5    Buchrieser, C.6    Hilbi, H.7
  • 47
    • 0037881861 scopus 로고    scopus 로고
    • KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system
    • Kitayama, Y., Iwasaki, H., Nishiwaki, T., and Kondo, T. (2003) KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system. EMBO J 22: 2127-2134.
    • (2003) EMBO J , vol.22 , pp. 2127-2134
    • Kitayama, Y.1    Iwasaki, H.2    Nishiwaki, T.3    Kondo, T.4
  • 48
    • 75749083323 scopus 로고    scopus 로고
    • Virulence factors encoded by Legionella longbeachae identified on the basis of the genome sequence analysis of clinical isolate D-4968
    • Kozak, N.A., Buss, M., Lucas, C.E., Frace, M., Govil, D., Travis, T., etal. (2010) Virulence factors encoded by Legionella longbeachae identified on the basis of the genome sequence analysis of clinical isolate D-4968. J Bacteriol 192: 1030-1044.
    • (2010) J Bacteriol , vol.192 , pp. 1030-1044
    • Kozak, N.A.1    Buss, M.2    Lucas, C.E.3    Frace, M.4    Govil, D.5    Travis, T.6
  • 50
    • 33749038907 scopus 로고    scopus 로고
    • Compensatory functions of two alkyl hydroperoxide reductases in the oxidative defense system of Legionella pneumophila
    • LeBlanc, J.J., Davidson, R.J., and Hoffman, P.S. (2006) Compensatory functions of two alkyl hydroperoxide reductases in the oxidative defense system of Legionella pneumophila. J Bacteriol 188: 6235-6244.
    • (2006) J Bacteriol , vol.188 , pp. 6235-6244
    • LeBlanc, J.J.1    Davidson, R.J.2    Hoffman, P.S.3
  • 51
    • 47049121331 scopus 로고    scopus 로고
    • An ortholog of OxyR in Legionella pneumophila is expressed postexponentially and negatively regulates the alkyl hydroperoxide reductase (ahpC2D) operon
    • LeBlanc, J.J., Brassinga, A.K., Ewann, F., Davidson, R.J., and Hoffman, P.S. (2008) An ortholog of OxyR in Legionella pneumophila is expressed postexponentially and negatively regulates the alkyl hydroperoxide reductase (ahpC2D) operon. J Bacteriol 190: 3444-3455.
    • (2008) J Bacteriol , vol.190 , pp. 3444-3455
    • LeBlanc, J.J.1    Brassinga, A.K.2    Ewann, F.3    Davidson, R.J.4    Hoffman, P.S.5
  • 52
    • 77953704524 scopus 로고    scopus 로고
    • The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication
    • Lomma, M., Dervins-Ravault, D., Rolando, M., Nora, T., Newton, H.J., Sansom, F.M., etal. (2010) The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication. Cell Microbiol 12: 1272-1291.
    • (2010) Cell Microbiol , vol.12 , pp. 1272-1291
    • Lomma, M.1    Dervins-Ravault, D.2    Rolando, M.3    Nora, T.4    Newton, H.J.5    Sansom, F.M.6
  • 54
    • 0017662282 scopus 로고
    • Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease
    • McDade, J.E., Shepard, C.C., Fraser, D.W., Tsai, T.R., Redus, M.A., and Dowdle, W.R. (1977) Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease. N Engl J Med 297: 1197-1203.
    • (1977) N Engl J Med , vol.297 , pp. 1197-1203
    • McDade, J.E.1    Shepard, C.C.2    Fraser, D.W.3    Tsai, T.R.4    Redus, M.A.5    Dowdle, W.R.6
  • 55
    • 77951921902 scopus 로고    scopus 로고
    • Mammalian Per-Arnt-Sim proteins in environmental adaptation
    • McIntosh, B.E., Hogenesch, J.B., and Bradfield, C.A. (2010) Mammalian Per-Arnt-Sim proteins in environmental adaptation. Annu Rev Physiol 72: 625-645.
    • (2010) Annu Rev Physiol , vol.72 , pp. 625-645
    • McIntosh, B.E.1    Hogenesch, J.B.2    Bradfield, C.A.3
  • 56
    • 34548496311 scopus 로고    scopus 로고
    • Winding up the cyanobacterial circadian clock
    • Mackey, S.R., and Golden, S.S. (2007) Winding up the cyanobacterial circadian clock. Trends Microbiol 1: 381-388.
    • (2007) Trends Microbiol , vol.1 , pp. 381-388
    • Mackey, S.R.1    Golden, S.S.2
  • 57
    • 80052872129 scopus 로고    scopus 로고
    • The itty-bitty time machine genetics of the cyanobacterial circadian clock
    • Mackey, S.R., Golden, S.S., and Ditty, J.L. (2011) The itty-bitty time machine genetics of the cyanobacterial circadian clock. Adv Genet 74: 13-53.
    • (2011) Adv Genet , vol.74 , pp. 13-53
    • Mackey, S.R.1    Golden, S.S.2    Ditty, J.L.3
  • 58
    • 12744269975 scopus 로고    scopus 로고
    • Rhythmic gene expression in a purple photosynthetic bacterium, Rhodobacter sphaeroide
    • Min, H., Guo, H., and Xiong, J. (2005a) Rhythmic gene expression in a purple photosynthetic bacterium, Rhodobacter sphaeroide. FEBS Lett 579: 808-812.
    • (2005) FEBS Lett , vol.579 , pp. 808-812
    • Min, H.1    Guo, H.2    Xiong, J.3
  • 59
    • 77950421915 scopus 로고    scopus 로고
    • Genome analysis of microorganisms living in amoebae reveals a melting pot of evolution
    • Moliner, C., Fournier, P.E., and Raoult, D. (2010) Genome analysis of microorganisms living in amoebae reveals a melting pot of evolution. FEMS Microbiol Rev 34: 281-294.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 281-294
    • Moliner, C.1    Fournier, P.E.2    Raoult, D.3
  • 60
    • 3142512687 scopus 로고    scopus 로고
    • Differentiate to thrive: lessons from the Legionella pneumophila life cycle
    • Molofsky, A.B., and Swanson, M.S. (2004) Differentiate to thrive: lessons from the Legionella pneumophila life cycle. Mol Microbiol 53: 29-40.
    • (2004) Mol Microbiol , vol.53 , pp. 29-40
    • Molofsky, A.B.1    Swanson, M.S.2
  • 61
    • 17244373578 scopus 로고    scopus 로고
    • Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro
    • Nakajima, M., Imai, K., Ito, H., Nishiwaki, T., Murayama, Y., Iwasaki, H., etal. (2005) Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro. Science 308: 414-415.
    • (2005) Science , vol.308 , pp. 414-415
    • Nakajima, M.1    Imai, K.2    Ito, H.3    Nishiwaki, T.4    Murayama, Y.5    Iwasaki, H.6
  • 62
    • 77950662773 scopus 로고    scopus 로고
    • Molecular pathogenesis of infections caused by Legionella pneumophila
    • Newton, H.J., Ang, D.K., van Driel, I.R., and Hartland, E.L. (2010) Molecular pathogenesis of infections caused by Legionella pneumophila. Clin Microbiol Rev 23: 274-298.
    • (2010) Clin Microbiol Rev , vol.23 , pp. 274-298
    • Newton, H.J.1    Ang, D.K.2    van Driel, I.R.3    Hartland, E.L.4
  • 63
    • 0034602708 scopus 로고    scopus 로고
    • Nucleotide binding and autophosphorylation of the clock protein KaiC as a circadian timing process of cyanobacteria
    • Nishiwaki, T., Iwasaki, H., Ishiura, M., and Kondo, T. (2000) Nucleotide binding and autophosphorylation of the clock protein KaiC as a circadian timing process of cyanobacteria. Proc Natl Acad Sci USA 97: 495-499.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 495-499
    • Nishiwaki, T.1    Iwasaki, H.2    Ishiura, M.3    Kondo, T.4
  • 64
    • 34548382214 scopus 로고    scopus 로고
    • A sequential program of dual phosphorylation of KaiC as a basis for circadian rhythm in cyanobacteria
    • Nishiwaki, T., Satomi, Y., Kitayama, Y., Terauchi, K., Kiyohara, R., Takao, T., and Kondo, T. (2007) A sequential program of dual phosphorylation of KaiC as a basis for circadian rhythm in cyanobacteria. EMBO J 26: 4029-4037.
    • (2007) EMBO J , vol.26 , pp. 4029-4037
    • Nishiwaki, T.1    Satomi, Y.2    Kitayama, Y.3    Terauchi, K.4    Kiyohara, R.5    Takao, T.6    Kondo, T.7
  • 65
    • 84863242725 scopus 로고    scopus 로고
    • Draft genome sequences of two Legionella dumoffii strains, TEX-KL and NY-23
    • Qin, T., Cui, Y., Cen, Z., Liang, T., Ren, H., Yang, X., etal. (2012) Draft genome sequences of two Legionella dumoffii strains, TEX-KL and NY-23. J Bacteriol 194: 1251-1252.
    • (2012) J Bacteriol , vol.194 , pp. 1251-1252
    • Qin, T.1    Cui, Y.2    Cen, Z.3    Liang, T.4    Ren, H.5    Yang, X.6
  • 67
    • 0036081333 scopus 로고    scopus 로고
    • Macrophage-induced genes of Legionella pneumophila: protection from reactive intermediates and solute imbalance during intracellular growth
    • Rankin, S., Li, Z., and Isberg, R.R. (2002) Macrophage-induced genes of Legionella pneumophila: protection from reactive intermediates and solute imbalance during intracellular growth. Infect Immun 70: 3637-3648.
    • (2002) Infect Immun , vol.70 , pp. 3637-3648
    • Rankin, S.1    Li, Z.2    Isberg, R.R.3
  • 68
    • 0036785675 scopus 로고    scopus 로고
    • Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection
    • Robey, M., and Cianciotto, N. (2002) Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection. Infect Immun 70: 5659-5669.
    • (2002) Infect Immun , vol.70 , pp. 5659-5669
    • Robey, M.1    Cianciotto, N.2
  • 69
    • 84876395478 scopus 로고    scopus 로고
    • Legionella pneumophila effector RomA uniquely modifies host chromatin to repress gene expression and promote intracellular bacterial replication
    • Rolando, M., Sanulli, S., Rusniok, C., Gomez-Valzero, L., Bertholet, C., Sahr, T., etal. (2013) Legionella pneumophila effector RomA uniquely modifies host chromatin to repress gene expression and promote intracellular bacterial replication. Cell Host Microbe 13: 395-405.
    • (2013) Cell Host Microbe , vol.13 , pp. 395-405
    • Rolando, M.1    Sanulli, S.2    Rusniok, C.3    Gomez-Valzero, L.4    Bertholet, C.5    Sahr, T.6
  • 70
    • 37549018348 scopus 로고    scopus 로고
    • Ordered phosphorylation governs oscillation of a three-protein circadian clock
    • Rust, M.J., Markson, J.S., Lane, W.S., Fisher, D.S., and O'Shea, E.K. (2007) Ordered phosphorylation governs oscillation of a three-protein circadian clock. Science 318: 809-812.
    • (2007) Science , vol.318 , pp. 809-812
    • Rust, M.J.1    Markson, J.S.2    Lane, W.S.3    Fisher, D.S.4    O'Shea, E.K.5
  • 72
    • 84860771585 scopus 로고    scopus 로고
    • Deep sequencing defines the transcriptional map of L. pneumophila and identifies growth phase-dependent regulated ncRNAs implicated in virulence
    • Sahr, T., Rusniok, C., Dervins-Ravault, D., Sismeiro, O., Coppee, J.Y., and Buchrieser, C. (2012) Deep sequencing defines the transcriptional map of L. pneumophila and identifies growth phase-dependent regulated ncRNAs implicated in virulence. RNA Biol 9: 503-519.
    • (2012) RNA Biol , vol.9 , pp. 503-519
    • Sahr, T.1    Rusniok, C.2    Dervins-Ravault, D.3    Sismeiro, O.4    Coppee, J.Y.5    Buchrieser, C.6
  • 73
    • 0029864850 scopus 로고    scopus 로고
    • Periplasmic copper-zinc superoxide dismutase of Legionella pneumophila: role in stationary-phase survival
    • St John, G., and Steinman, H.M. (1996) Periplasmic copper-zinc superoxide dismutase of Legionella pneumophila: role in stationary-phase survival. J Bacteriol 178: 1578-1584.
    • (1996) J Bacteriol , vol.178 , pp. 1578-1584
    • St John, G.1    Steinman, H.M.2
  • 74
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer, T., and Jenal, U. (2009) Structural and mechanistic determinants of c-di-GMP signalling. Nat Rev Microbiol 7: 724-735.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 75
    • 0345118289 scopus 로고    scopus 로고
    • Photochemical effects on microbial activity in natural waters: the interaction of reactive oxygen species and dissolved organic matter
    • Scully, N.M., Cooper, W.J., and Tranvik, L.J. (2003) Photochemical effects on microbial activity in natural waters: the interaction of reactive oxygen species and dissolved organic matter. FEMS Microbiol Ecol 46: 353-357.
    • (2003) FEMS Microbiol Ecol , vol.46 , pp. 353-357
    • Scully, N.M.1    Cooper, W.J.2    Tranvik, L.J.3
  • 76
    • 33744779947 scopus 로고    scopus 로고
    • Circadian rhythms in gene transcription imparted by chromosome compaction in the cyanobacterium Synechococcus elongatus
    • Smith, R.M., and Williams, S.B. (2006) Circadian rhythms in gene transcription imparted by chromosome compaction in the cyanobacterium Synechococcus elongatus. Proc Natl Acad Sci USA 103: 8564-8569.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8564-8569
    • Smith, R.M.1    Williams, S.B.2
  • 77
    • 0033056903 scopus 로고    scopus 로고
    • The pvc gene cluster of Pseudomonas aeruginosa: role in synthesis of the pyoverdine chromophore and regulation by PtxR and PvdS
    • Stintzi, A., Johnson, Z., Stonehouse, M., Ochsner, U., Meyer, J.M., Vasil, M.L., and Poole, K. (1999) The pvc gene cluster of Pseudomonas aeruginosa: role in synthesis of the pyoverdine chromophore and regulation by PtxR and PvdS. J Bacteriol 181: 4118-4124.
    • (1999) J Bacteriol , vol.181 , pp. 4118-4124
    • Stintzi, A.1    Johnson, Z.2    Stonehouse, M.3    Ochsner, U.4    Meyer, J.M.5    Vasil, M.L.6    Poole, K.7
  • 78
    • 80054796108 scopus 로고    scopus 로고
    • Using the T-coffee package to build multiple sequence alignments of protein, RNA, DNA sequences and 3D structures
    • Taly, J.F., Magis, C., Bussotti, G., Chang, J.M., Tommaso, P.D., Erb, I., etal. (2011) Using the T-coffee package to build multiple sequence alignments of protein, RNA, DNA sequences and 3D structures. Nat Protoc 6: 1669-1682.
    • (2011) Nat Protoc , vol.6 , pp. 1669-1682
    • Taly, J.F.1    Magis, C.2    Bussotti, G.3    Chang, J.M.4    Tommaso, P.D.5    Erb, I.6
  • 79
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 80
    • 33846150032 scopus 로고    scopus 로고
    • labA: a novel gene required for negative feedback regulation of the cyanobacterial circadian clock protein KaiC
    • Taniguchi, Y., Katayama, M., Ito, R., Takai, N., Kondo, T., and Oyama, T. (2007) labA: a novel gene required for negative feedback regulation of the cyanobacterial circadian clock protein KaiC. Genes Dev 21: 60-70.
    • (2007) Genes Dev , vol.21 , pp. 60-70
    • Taniguchi, Y.1    Katayama, M.2    Ito, R.3    Takai, N.4    Kondo, T.5    Oyama, T.6
  • 81
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor, B.L., and Zhulin, I.B. (1999) PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63: 479-506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 82
    • 84871732305 scopus 로고    scopus 로고
    • The circadian clock-associated small GTPase LIGHT INSENSITIVE PERIOD1 suppresses light-controlled endoreplication and affects tolerance to salt stress in Arabidopsis
    • Terecskei, K., Tóth, R., Gyula, P., Kevei, E., Bindics, J., Coupland, G., etal. (2013) The circadian clock-associated small GTPase LIGHT INSENSITIVE PERIOD1 suppresses light-controlled endoreplication and affects tolerance to salt stress in Arabidopsis. Plant Physiol 161: 278-290.
    • (2013) Plant Physiol , vol.161 , pp. 278-290
    • Terecskei, K.1    Tóth, R.2    Gyula, P.3    Kevei, E.4    Bindics, J.5    Coupland, G.6
  • 84
    • 12244296161 scopus 로고    scopus 로고
    • No transcription-translation feedback in circadian rhythm of KaiC phosphorylation
    • Tomita, J., Nakajima, M., Kondo, T., and Iwasaki, H. (2005) No transcription-translation feedback in circadian rhythm of KaiC phosphorylation. Science 307: 251-254.
    • (2005) Science , vol.307 , pp. 251-254
    • Tomita, J.1    Nakajima, M.2    Kondo, T.3    Iwasaki, H.4
  • 85
    • 84934444524 scopus 로고    scopus 로고
    • Expression and purification of soluble His(6)-tagged TEV protease
    • Tropea, J.E., Cherry, S., and Waugh, D.S. (2009) Expression and purification of soluble His(6)-tagged TEV protease. Methods Mol Biol 498: 297-307.
    • (2009) Methods Mol Biol , vol.498 , pp. 297-307
    • Tropea, J.E.1    Cherry, S.2    Waugh, D.S.3
  • 86
    • 84892986955 scopus 로고
    • Basic Population Genetics. In. New York: Columbia University
    • Wallace, B. (1981) Basic Population Genetics. In. New York: Columbia University, pp.
    • (1981)
    • Wallace, B.1
  • 87
    • 84876931666 scopus 로고    scopus 로고
    • Biochemical analysis of three putative KaiC clock proteins from Synechocystis sp. PCC 6803 suggests their functional divergence
    • Wiegard, A., Dorrich, A.K., Deinzer, H.T., Beck, C., Wilde, A., Holtzendorff, J., and Axmann, I.M. (2013) Biochemical analysis of three putative KaiC clock proteins from Synechocystis sp. PCC 6803 suggests their functional divergence. Microbiology 159: 948-958.
    • (2013) Microbiology , vol.159 , pp. 948-958
    • Wiegard, A.1    Dorrich, A.K.2    Deinzer, H.T.3    Beck, C.4    Wilde, A.5    Holtzendorff, J.6    Axmann, I.M.7
  • 88
    • 4344699146 scopus 로고    scopus 로고
    • The adaptive value of circadian clocks: an experimental assessment in cyanobacteria
    • Woelfle, M.A., Ouyang, Y., Phanvijhitsiri, K., and Johnson, C.H. (2004) The adaptive value of circadian clocks: an experimental assessment in cyanobacteria. Curr Biol 14: 1481-1486.
    • (2004) Curr Biol , vol.14 , pp. 1481-1486
    • Woelfle, M.A.1    Ouyang, Y.2    Phanvijhitsiri, K.3    Johnson, C.H.4
  • 89
    • 0035190121 scopus 로고    scopus 로고
    • Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase
    • Zhang, R.G., Skarina, T., Katz, J.E., Beasley, S., Khachatryan, A., Vyas, S., etal. (2001) Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure 9: 1095-1106.
    • (2001) Structure , vol.9 , pp. 1095-1106
    • Zhang, R.G.1    Skarina, T.2    Katz, J.E.3    Beasley, S.4    Khachatryan, A.5    Vyas, S.6
  • 90
    • 0036136235 scopus 로고    scopus 로고
    • Characterization of a Legionella pneumophila relA insertion mutant and toles of RelA and RpoS in virulence gene expression
    • Zusman, T., Gal-Mor, O., and Segal, G. (2002) Characterization of a Legionella pneumophila relA insertion mutant and toles of RelA and RpoS in virulence gene expression. J Bacteriol 184: 67-75.
    • (2002) J Bacteriol , vol.184 , pp. 67-75
    • Zusman, T.1    Gal-Mor, O.2    Segal, G.3


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