메뉴 건너뛰기




Volumn 156, Issue 9, 2010, Pages 2873-2886

Escherichia coli K-12 YfgF is an anaerobic cyclic di-GMP phosphodiesterase with roles in cell surface remodelling and the oxidative stress response

Author keywords

[No Author keywords available]

Indexed keywords

5' PHOSPHOGUANYLYL(3 5')GUANOSINE; BACTERIAL PROTEIN; CYCLIC GMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; GUANOSINE; MAGNESIUM ION; PROTEIN YGFG; UNCLASSIFIED DRUG;

EID: 77956357900     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.037887-0     Document Type: Article
Times cited : (31)

References (73)
  • 1
    • 23844484214 scopus 로고    scopus 로고
    • Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S] FNR of Escherichia coli
    • Achebach, S., Selmer, T. & Unden, G. (2005). Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S] FNR of Escherichia coli. FEBS J 272, 4260-4269.
    • (2005) FEBS J , vol.272 , pp. 4260-4269
    • Achebach, S.1    Selmer, T.2    Unden, G.3
  • 2
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem, A., Varghese, S. & Imlay, J. I. (2009). Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol Microbiol 72, 844-858.
    • (2009) Mol Microbiol , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.I.3
  • 3
    • 76649134086 scopus 로고    scopus 로고
    • Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole cell assays suitable for high-throughput screening of biofilm inhibitors
    • Antoniani, D., Bocci, P., Maciag, A., Raffaelli, N. & Landini, P. (2010). Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole cell assays suitable for high-throughput screening of biofilm inhibitors. Appl Microbiol Biotechnol 85, 1095-1104.
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1095-1104
    • Antoniani, D.1    Bocci, P.2    Maciag, A.3    Raffaelli, N.4    Landini, P.5
  • 4
    • 0010870712 scopus 로고    scopus 로고
    • Secrets of bacterial transcription initiation taught by the Escherichia coli FNR protein
    • Edited by D. A. Hodgson & C. M. Thomas. Cambridge, UK: Cambridge University Press
    • Browning, D., Lee, D., Green, J. & Busby, S. (2003). Secrets of bacterial transcription initiation taught by the Escherichia coli FNR protein. In Signals, Switches, Regulons and Cascades: Control of Bacterial Gene Expression, pp. 127-142. Edited by D. A. Hodgson & C. M. Thomas. Cambridge, UK: Cambridge University Press.
    • (2003) Signals, Switches, Regulons and Cascades: Control of Bacterial Gene Expression , pp. 127-142
    • Browning, D.1    Lee, D.2    Green, J.3    Busby, S.4
  • 7
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • Christen, M., Christen, B., Folcher, M., Schauerte, A. & Jenal, U. (2005). Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J Biol Chem 280, 30829-30837.
    • (2005) J Biol Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 9
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G. & von Heijne, G. (1994). TopPred II: an improved software for membrane protein structure predictions. Comput Appl Biosci 10, 685-686.
    • (1994) Comput Appl Biosci , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 10
    • 33646184857 scopus 로고    scopus 로고
    • A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL and NarPQ as Escherichia coli adapts from aerobic to anaerobic growth
    • Constantinidou, C., Hobman, J. L., Griffiths, L., Patel, M. D., Penn, C. W., Cole, J. A. & Overton, T. W. (2006). A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL and NarPQ as Escherichia coli adapts from aerobic to anaerobic growth. J Biol Chem 281, 4802-4815.
    • (2006) J Biol Chem , vol.281 , pp. 4802-4815
    • Constantinidou, C.1    Hobman, J.L.2    Griffiths, L.3    Patel, M.D.4    Penn, C.W.5    Cole, J.A.6    Overton, T.W.7
  • 11
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS domain protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon, V. M., Gonzalez, G. & Gilles-Gonzalez, M. A. (2000). Dos, a heme-binding PAS domain protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39, 2685-2691.
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 12
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig, A., Abel, S., Folcher, M., Nicollier, M., Schwede, T., Amiot, N., Giese, B. & Jenal, U. (2009). Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 23, 93-104.
    • (2009) Genes Dev , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6    Giese, B.7    Jenal, U.8
  • 14
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin, M. Y., Nikolskaya, A. N. & Koonin, E. V. (2001). Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 203, 11-21.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 15
    • 34848889244 scopus 로고    scopus 로고
    • A comprehensive genetic characterization of bacterial motility
    • Girgis, H. S., Liu, Y., Ryu, W. S. & Tavazoie, S. (2007). A comprehensive genetic characterization of bacterial motility. PLoS Genet 3, 1644-1660.
    • (2007) PLoS Genet , vol.3 , pp. 1644-1660
    • Girgis, H.S.1    Liu, Y.2    Ryu, W.S.3    Tavazoie, S.4
  • 16
    • 9444239308 scopus 로고    scopus 로고
    • Bacterial redox sensors
    • Green, J. & Paget, M. S. (2004). Bacterial redox sensors. Nat Rev Microbiol 2, 954-966.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 954-966
    • Green, J.1    Paget, M.S.2
  • 18
    • 0028016327 scopus 로고
    • Dimorphic transition in Escherichia coli and Salmonella typhimurium: Surface-induced differentiation into hyperflagellate swarmer cells
    • Harshey, R. M. & Matsuyama, T. (1994). Dimorphic transition in Escherichia coli and Salmonella typhimurium: surface-induced differentiation into hyperflagellate swarmer cells. Proc Natl Acad Sci U S A 91, 8631-8635.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8631-8635
    • Harshey, R.M.1    Matsuyama, T.2
  • 19
    • 0028844985 scopus 로고
    • Identification of a novel response regulator required for the swarmer-to-stalked cell transition in Caulobacter crescentus
    • Hecht, G. B. & Newton, A. (1995). Identification of a novel response regulator required for the swarmer-to-stalked cell transition in Caulobacter crescentus. J Bacteriol 177, 6223-6229.
    • (1995) J Bacteriol , vol.177 , pp. 6223-6229
    • Hecht, G.B.1    Newton, A.2
  • 20
    • 19944422767 scopus 로고    scopus 로고
    • A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial virulence in mice, anti-oxidant defence and killing of macrophages: Role of cyclic-diGMP
    • Hisert, K. B., MacCoss, M., Shiloh, M. U., Darwin, K. H., Singh, S., Jones, R. A., Ehrt, S., Zhang, Z., Gaffney, B. L. & other authors (2005). A glutamate-alanine-leucine (EAL) domain protein of Salmonella controls bacterial virulence in mice, anti-oxidant defence and killing of macrophages: role of cyclic-diGMP. Mol Microbiol 56, 1234-1245.
    • (2005) Mol Microbiol , vol.56 , pp. 1234-1245
    • Hisert, K.B.1    MacCoss, M.2    Shiloh, M.U.3    Darwin, K.H.4    Singh, S.5    Jones, R.A.6    Ehrt, S.7    Zhang, Z.8    Gaffney, B.L.9
  • 21
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hoffmann, K. & Stoffel, W. (1993). TMbase - a database of membrane spanning protein segments. Biol Chem Hoppe Seyler 374, 166.
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hoffmann, K.1    Stoffel, W.2
  • 22
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic diguanosine monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria?
    • Jenal, U. (2004). Cyclic diguanosine monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria? Curr Opin Microbiol 7, 185-191.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 185-191
    • Jenal, U.1
  • 23
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signalling in bacteria
    • Jenal, U. & Malone, J. (2006). Mechanisms of cyclic-di-GMP signalling in bacteria. Annu Rev Genet 40, 385-407.
    • (2006) Annu Rev Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 26
    • 13244289800 scopus 로고    scopus 로고
    • Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function
    • Kang, Y., Weber, K. D., Qiu, Y., Kiley, P. J. & Blattner, F. R. (2005). Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function. J Bacteriol 187, 1135-1160.
    • (2005) J Bacteriol , vol.187 , pp. 1135-1160
    • Kang, Y.1    Weber, K.D.2    Qiu, Y.3    Kiley, P.J.4    Blattner, F.R.5
  • 27
    • 0037893024 scopus 로고    scopus 로고
    • The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen
    • Kehres, D. G., Zaharik, M. L., Finlay, B. B. & Maguire, M. E. (2000). The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen. Mol Microbiol 36, 1085-1100.
    • (2000) Mol Microbiol , vol.36 , pp. 1085-1100
    • Kehres, D.G.1    Zaharik, M.L.2    Finlay, B.B.3    Maguire, M.E.4
  • 28
    • 33644516891 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence
    • Kulasakara, H., Lee, V., Brencic, A., Liberati, N., Urbach, J., Miyata, S., Lee, D. G., Neely, A. N., Hyodo, M. & other authors (2006). Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence. Proc Natl Acad Sci U S A 103, 2839-2844.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2839-2844
    • Kulasakara, H.1    Lee, V.2    Brencic, A.3    Liberati, N.4    Urbach, J.5    Miyata, S.6    Lee, D.G.7    Neely, A.N.8    Hyodo, M.9
  • 29
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., Beinert, H., Khoroshilova, N., Kennedy, M. C. & Kiley, P. J. (1996). DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 271, 2762-2768.
    • (1996) J Biol Chem , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 30
    • 34548303826 scopus 로고    scopus 로고
    • A cyclic-di-GMP receptor required for bacterial exopolysaccharide production
    • Lee, V. T., Matewish, J. M., Kessler, J. L., Hyodo, M., Hayakowa, Y. & Lory, S. (2007). A cyclic-di-GMP receptor required for bacterial exopolysaccharide production. Mol Microbiol 65, 1474-1484.
    • (2007) Mol Microbiol , vol.65 , pp. 1474-1484
    • Lee, V.T.1    Matewish, J.M.2    Kessler, J.L.3    Hyodo, M.4    Hayakowa, Y.5    Lory, S.6
  • 31
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E. S. (1955). Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 32
    • 0023787932 scopus 로고
    • PACYC184-derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids
    • Martinez, E., Bartolome, B. & Delacruz, F. (1988). pACYC184-derived cloning vectors containing the multiple cloning site and lacZα reporter gene of pUC8/9 and pUC18/19 plasmids. Gene 68, 159-162.
    • (1988) Gene , vol.68 , pp. 159-162
    • Martinez, E.1    Bartolome, B.2    Delacruz, F.3
  • 34
    • 0030997843 scopus 로고    scopus 로고
    • FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites
    • Meng, W., Green, J. & Guest, J. R. (1997). FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites. Microbiology 143, 1521-1532.
    • (1997) Microbiology , vol.143 , pp. 1521-1532
    • Meng, W.1    Green, J.2    Guest, J.R.3
  • 35
    • 0002972659 scopus 로고
    • Assay of β-galactosidase
    • Edited by J. H. Miller. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Miller, J. H. (1972). Assay of β-galactosidase. In Experiments in Molecular Genetics, pp. 352-355. Edited by J. H. Miller. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 37
    • 33748769255 scopus 로고    scopus 로고
    • Escherichia coli transcriptome dynamics during the transition from anaerobic to aerobic conditions
    • Partridge, J. D., Scott, C., Tang, Y., Poole, R. K. & Green, J. (2006). Escherichia coli transcriptome dynamics during the transition from anaerobic to aerobic conditions. J Biol Chem 281, 27806-27815.
    • (2006) J Biol Chem , vol.281 , pp. 27806-27815
    • Partridge, J.D.1    Scott, C.2    Tang, Y.3    Poole, R.K.4    Green, J.5
  • 38
    • 34249110125 scopus 로고    scopus 로고
    • The Escherichia coli yhjA gene, encoding a predicted cytochrome c peroxidase, is regulated by FNR and OxyR
    • Partridge, J. D., Poole, R. K. & Green, J. (2007a). The Escherichia coli yhjA gene, encoding a predicted cytochrome c peroxidase, is regulated by FNR and OxyR. Microbiology 153, 1499-1509.
    • (2007) Microbiology , vol.153 , pp. 1499-1509
    • Partridge, J.D.1    Poole, R.K.2    Green, J.3
  • 39
    • 34249727710 scopus 로고    scopus 로고
    • Transition of Escherichia coli from aerobic to micro-aerobic conditions involves fast and slow reacting regulatory components
    • Partridge, J. D., Sanguinetti, G., Dibden, D. P., Roberts, R. E., Poole, R. K. & Green, J. (2007b). Transition of Escherichia coli from aerobic to micro-aerobic conditions involves fast and slow reacting regulatory components. J Biol Chem 282, 11230-11237.
    • (2007) J Biol Chem , vol.282 , pp. 11230-11237
    • Partridge, J.D.1    Sanguinetti, G.2    Dibden, D.P.3    Roberts, R.E.4    Poole, R.K.5    Green, J.6
  • 40
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul, R., Weiser, S., Amiot, N. C., Chan, C., Schirmer, T., Giese, B. & Jenal, U. (2004). Cell cycle dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev 18, 715-727.
    • (2004) Genes Dev , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 41
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
    • Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H. & Jenal, U. (2007). Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J Biol Chem 282, 29170-29177.
    • (2007) J Biol Chem , vol.282 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 42
    • 0035254950 scopus 로고    scopus 로고
    • GGDEF domain is homologous to adenylyl cyclase
    • Pei, J. & Grishin, N. V. (2001). GGDEF domain is homologous to adenylyl cyclase. Proteins 42, 210-216.
    • (2001) Proteins , vol.42 , pp. 210-216
    • Pei, J.1    Grishin, N.V.2
  • 43
    • 63749115101 scopus 로고    scopus 로고
    • Bacterial nucleotide-based second messengers
    • Pesavento, C. & Hengge, R. (2009). Bacterial nucleotide-based second messengers. Curr Opin Microbiol 12, 170-176.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 170-176
    • Pesavento, C.1    Hengge, R.2
  • 44
    • 51149098349 scopus 로고    scopus 로고
    • Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli
    • Pesavento, C., Becker, G., Sommerfeldt, N., Possling, A., Tschowri, N., Mehlis, A. & Hengge, R. (2008). Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli. Genes Dev 22, 2434-2446.
    • (2008) Genes Dev , vol.22 , pp. 2434-2446
    • Pesavento, C.1    Becker, G.2    Sommerfeldt, N.3    Possling, A.4    Tschowri, N.5    Mehlis, A.6    Hengge, R.7
  • 45
    • 0021355708 scopus 로고
    • λ Red-dependent growth and recombination of phage P22
    • Poteete, A. R. & Fenton, A. C. (1984). λ red-dependent growth and recombination of phage P22. Virology 134, 161-167.
    • (1984) Virology , vol.134 , pp. 161-167
    • Poteete, A.R.1    Fenton, A.C.2
  • 47
    • 33645894689 scopus 로고    scopus 로고
    • Cyclic-di-GMP as a second messenger
    • Römling, U. & Amikam, D. (2006). Cyclic-di-GMP as a second messenger. Curr Opin Microbiol 9, 218-228.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 218-228
    • Römling, U.1    Amikam, D.2
  • 49
    • 33845400857 scopus 로고    scopus 로고
    • Cyclic-di-GMP signalling in bacteria: Recent advances and new puzzles
    • Ryan, R. P., Fouhy, Y., Lucey, J. F. & Dow, J. M. (2006). Cyclic-di-GMP signalling in bacteria: recent advances and new puzzles. J Bacteriol 188, 8327-8334.
    • (2006) J Bacteriol , vol.188 , pp. 8327-8334
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3    Dow, J.M.4
  • 50
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov, D. A., Tarutina, M., Moskvin, O. M. & Gomelsky, M. (2005). Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J Bacteriol 187, 1792-1798.
    • (2005) J Bacteriol , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.M.3    Gomelsky, M.4
  • 51
    • 33750044865 scopus 로고    scopus 로고
    • The PilZ domain is a receptor for the second messenger c-di-GMP: The PilZ domain protein YcgR controls motility in enterobacteria
    • Ryjenkov, D. A., Simm, R., Römling, U. & Gomelsky, M. (2006). The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria. J Biol Chem 281, 30310-30314.
    • (2006) J Biol Chem , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Römling, U.3    Gomelsky, M.4
  • 52
    • 0043032584 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12: The effects of oxygen availability and FNR
    • Salmon, K., Hung, S. P., Mekjian, K., Baldi, P., Hatfield, G. W. & Gunsalus, R. P. (2003). Global gene expression profiling in Escherichia coli K12: the effects of oxygen availability and FNR. J Biol Chem 278, 29837-29855.
    • (2003) J Biol Chem , vol.278 , pp. 29837-29855
    • Salmon, K.1    Hung, S.P.2    Mekjian, K.3    Baldi, P.4    Hatfield, G.W.5    Gunsalus, R.P.6
  • 54
    • 0037189552 scopus 로고    scopus 로고
    • Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of heme redox states and mutations at the heme binding site on catalysis and structure
    • Sasakura, Y., Hirata, S., Sugiyama, S., Suzuki, S., Taguchi, S., Watanabe, M., Matsui, T., Sagami, I. & Shimizu, T. (2002). Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of heme redox states and mutations at the heme binding site on catalysis and structure. J Biol Chem 277, 23821-23827.
    • (2002) J Biol Chem , vol.277 , pp. 23821-23827
    • Sasakura, Y.1    Hirata, S.2    Sugiyama, S.3    Suzuki, S.4    Taguchi, S.5    Watanabe, M.6    Matsui, T.7    Sagami, I.8    Shimizu, T.9
  • 55
    • 21844451590 scopus 로고    scopus 로고
    • Ubiquitous protein domain EAL encodes cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt, A. J., Ryjenkov, D. A. & Gomelsky, M. (2005). Ubiquitous protein domain EAL encodes cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J Bacteriol 187, 4774-4781.
    • (2005) J Bacteriol , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 56
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic-di-GMP levels and transition from sessility to motility
    • Simm, R., Morr, M., Kader, A., Nimtz, M. & Römling, U. (2004). GGDEF and EAL domains inversely regulate cyclic-di-GMP levels and transition from sessility to motility. Mol Microbiol 53, 1123-1134.
    • (2004) Mol Microbiol , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Römling, U.5
  • 57
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., Houman, F. & Kleckner, N. (1987). Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53, 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 58
    • 66049142620 scopus 로고    scopus 로고
    • Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signalling network in Salmonella
    • Solano, C., Garcia, B., Latasa, C., Toledo-Arana, A., Zorraquino, V., Valle, J., Casals, J., Pedroso, E. & Lasa, I. (2009). Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signalling network in Salmonella. Proc Natl Acad Sci U S A 106, 7997-8002.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7997-8002
    • Solano, C.1    Garcia, B.2    Latasa, C.3    Toledo-Arana, A.4    Zorraquino, V.5    Valle, J.6    Casals, J.7    Pedroso, E.8    Lasa, I.9
  • 59
    • 61449200221 scopus 로고    scopus 로고
    • Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli
    • Sommerfeldt, N., Possling, A., Becker, G., Pesavento, C., Tschowri, N. & Hengge, R. (2009). Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli. Microbiology 155, 1318-1331.
    • (2009) Microbiology , vol.155 , pp. 1318-1331
    • Sommerfeldt, N.1    Possling, A.2    Becker, G.3    Pesavento, C.4    Tschowri, N.5    Hengge, R.6
  • 60
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Sonnhammer, E. L., von Heijne, G. & Krogh, A. (1998). A hidden Markov model for predicting transmembrane helices in protein sequences. Proc Int Conf Intell Syst Mol Biol 6, 175-182.
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 175-182
    • Sonnhammer, E.L.1    Von Heijne, G.2    Krogh, A.3
  • 61
    • 0023571178 scopus 로고
    • Regulation and over-expression of the fnr gene of Escherichia coli
    • Spiro, S. & Guest, J. R. (1987). Regulation and over-expression of the fnr gene of Escherichia coli. J Gen Microbiol 133, 3279-3288.
    • (1987) J Gen Microbiol , vol.133 , pp. 3279-3288
    • Spiro, S.1    Guest, J.R.2
  • 62
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulator RNAs CsrB and CsrC for degradation by RNase E
    • Suzuki, K., Babitzke, P., Kushner, S. R. & Romeo, T. (2006). Identification of a novel regulatory protein (CsrD) that targets the global regulator RNAs CsrB and CsrC for degradation by RNase E. Genes Dev 20, 2605-2617.
    • (2006) Genes Dev , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 63
    • 0031783181 scopus 로고    scopus 로고
    • Three cdg operons control cellular turnover of cyclic-di-GMP in Acetobacter xylinum: Genetic organization and occurrence of conserved domains in isoenzymes
    • Tal, R., Wong, H. C., Calhoon, R., Gelfand, D., Fear, A. L., Volman, G., Mayer, R., Ross, P., Amikan, D. & other authors (1998). Three cdg operons control cellular turnover of cyclic-di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes. J Bacteriol 180, 4416-4425.
    • (1998) J Bacteriol , vol.180 , pp. 4416-4425
    • Tal, R.1    Wong, H.C.2    Calhoon, R.3    Gelfand, D.4    Fear, A.L.5    Volman, G.6    Mayer, R.7    Ross, P.8    Amikan, D.9
  • 64
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • Tamayo, R., Tischler, A. D. & Camilli, A. (2005). The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J Biol Chem 280, 33324-33330.
    • (2005) J Biol Chem , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 65
    • 34547137430 scopus 로고    scopus 로고
    • 95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP
    • 95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP. J Biol Chem 282, 21301-21307.
    • (2007) J Biol Chem , vol.282 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 66
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler, A. D. & Camilli, A. (2004). Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol Microbiol 53, 857-869.
    • (2004) Mol Microbiol , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 67
    • 23944431512 scopus 로고    scopus 로고
    • Cyclic diguanylate regulates Vibrio cholerae virulence gene expression
    • Tischler, A. D. & Camilli, A. (2005). Cyclic diguanylate regulates Vibrio cholerae virulence gene expression. Infect Immun 73, 5873-5882.
    • (2005) Infect Immun , vol.73 , pp. 5873-5882
    • Tischler, A.D.1    Camilli, A.2
  • 70
    • 0028853643 scopus 로고
    • Spacing requirements for transcription activation by Escherichia coli FNR protein
    • Wing, H. J., Williams, S. M. & Busby, S. J. W. (1995). Spacing requirements for transcription activation by Escherichia coli FNR protein. J Bacteriol 177, 6704-6710.
    • (1995) J Bacteriol , vol.177 , pp. 6704-6710
    • Wing, H.J.1    Williams, S.M.2    Busby, S.J.W.3
  • 71
    • 0034595406 scopus 로고    scopus 로고
    • A hemerythrin-like domain in a bacterial chemotaxis protein
    • Xiong, J., Kurtz, D. M., Jr, Ai, J. & Sanders-Loehr, J. (2000). A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39, 5117-5125.
    • (2000) Biochemistry , vol.39 , pp. 5117-5125
    • Xiong, J.1    Kurtz Jr., D.M.2    Ai, J.3    Sanders-Loehr, J.4
  • 73
    • 0028931445 scopus 로고
    • In vitro analysis of a constitutively active mutant form of the Escherichia coli global transcription factor FNR
    • Ziegelhoffer, E. C. & Kiley, P. J. (1995). In vitro analysis of a constitutively active mutant form of the Escherichia coli global transcription factor FNR. J Mol Biol 245, 351-361.
    • (1995) J Mol Biol , vol.245 , pp. 351-361
    • Ziegelhoffer, E.C.1    Kiley, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.