메뉴 건너뛰기
Journal of Bacteriology
Volumn 198, Issue 1, 2016, Pages 77-90
Cyclic dI-GMP regulates type IV pilus-dependent motility in Myxococcus xanthus
Author keywords

[No Author keywords available]
Indexed keywords

BACTERIAL PROTEIN; CYCLIC DI GMP; CYCLIC GMP; EAL PROTEIN; GGDEF PROTEIN; HD GYP PROTEIN; UNCLASSIFIED DRUG; BACTERIAL SECRETION SYSTEM; BIS(3',5')-CYCLIC DIGUANYLIC ACID;
EID: 84953897473     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00281-15     Document Type: Article
Times cited : (42)
References (82)
  • 1
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: the first 25 years of a universal bacterial second messenger
    • Römling U, Galperin MY, Gomelsky M. 2013. Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol Mol Biol Rev 77:1-52. http://dx.doi.org/10.1128/MMBR.00043-12.
    • (2013) Microbiol Mol Biol Rev , vol.77 , pp. 1-52
    • Römling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 2
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge R. 2009. Principles of c-di-GMP signalling in bacteria. Nat Rev Microbiol 7:263-273. http://dx.doi.org/10.1038/nrmicro2109.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 263-273
    • Hengge, R.1
  • 3
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal U, Malone J. 2006. Mechanisms of cyclic-di-GMP signaling in bacteria. Annu Rev Genet 40:385-407. http://dx.doi.org/10.1146/annurev.genet.40.110405.090423.
    • (2006) Annu Rev Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 4
    • 84862527194 scopus 로고    scopus 로고
    • Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP
    • Krasteva PV, Giglio KM, Sondermann H. 2012. Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP. Protein Sci 21:929-948. http://dx.doi.org/10.1002/pro.2093.
    • (2012) Protein Sci , vol.21 , pp. 929-948
    • Krasteva, P.V.1    Giglio, K.M.2    Sondermann, H.3
  • 5
    • 84870208079 scopus 로고    scopus 로고
    • Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems
    • Boyd CD, O'Toole GA. 2012. Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems. Annu Rev Cell Dev Biol 28:439-462. http://dx.doi.org/10.1146/annurev-cellbio-101011-155705.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 439-462
    • Boyd, C.D.1    O'Toole, G.A.2
  • 6
    • 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 NC, 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. http://dx.doi.org/10.1101/gad.289504.
    • (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
  • 7
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
    • Ryjenkov DA, Tarutina M, Moskvin OV, 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. http://dx.doi.org/10.1128/JB.187.5.1792-1798.2005.
    • (2005) J Bacteriol , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 8
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains
    • Schmidt AJ, Ryjenkov DA, Gomelsky M. 2005. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J Bacteriol 187:4774-4781. http://dx.doi.org/10.1128/JB.187.14.4774-4781.2005.
    • (2005) J Bacteriol , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 9
    • 25144489145 scopus 로고    scopus 로고
    • The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
    • Tamayo R, Tischler AD, Camilli A. 2005. The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase. J Biol Chem 280:33324-33330. http://dx.doi.org/10.1074/jbc.M506500200.
    • (2005) J Biol Chem , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 11
    • 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. http://dx.doi.org/10.1074/jbc.M504429200.
    • (2005) J Biol Chem , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 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. http://dx.doi.org/10.1101/gad.502409.
    • (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
  • 13
    • 84862777062 scopus 로고    scopus 로고
    • The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus
    • Petters T, Zhang X, Nesper J, Treuner-Lange A, Gomez-Santos N, Hoppert M, Jenal U, Søgaard-Andersen L. 2012. The orphan histidine protein kinase SgmT is a c-di-GMP receptor and regulates composition of the extracellular matrix together with the orphan DNA binding response regulator DigR in Myxococcus xanthus. Mol Microbiol 84:147-165. http://dx.doi.org/10.1111/j.1365-2958.2012.08015.x.
    • (2012) Mol Microbiol , vol.84 , pp. 147-165
    • Petters, T.1    Zhang, X.2    Nesper, J.3    Treuner-Lange, A.4    Gomez-Santos, N.5    Hoppert, M.6    Jenal, U.7    Søgaard-Andersen, L.8
  • 14
    • 78951471881 scopus 로고    scopus 로고
    • Binding of cyclic diguanylate in the non-catalytic EAL domain of FimX induces a long-range conformational change
    • Qi Y, Chuah MLC, Dong X, Xie K, Luo Z, Tang K, Liang Z-X. 2011. Binding of cyclic diguanylate in the non-catalytic EAL domain of FimX induces a long-range conformational change. J Biol Chem 286:2910-2917. http://dx.doi.org/10.1074/jbc.M110.196220.
    • (2011) J Biol Chem , vol.286 , pp. 2910-2917
    • Qi, Y.1    Chuah, M.L.C.2    Dong, X.3    Xie, K.4    Luo, Z.5    Tang, K.6    Liang, Z.-X.7
  • 15
    • 62549150834 scopus 로고    scopus 로고
    • LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1
    • Newell PD, Monds RD, O'Toole GA. 2009. LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc Natl Acad Sci U S A 106:3461-3466. http://dx.doi.org/10.1073/pnas.0808933106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'Toole, G.A.3
  • 16
    • 68149172669 scopus 로고    scopus 로고
    • Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX
    • Navarro MV, De N, Bae N, Wang Q, Sondermann H. 2009. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure 17:1104-1116. http://dx.doi.org/10.1016/j.str.2009.06.010.
    • (2009) Structure , vol.17 , pp. 1104-1116
    • Navarro, M.V.1    De, N.2    Bae, N.3    Wang, Q.4    Sondermann, H.5
  • 17
    • 75749118268 scopus 로고    scopus 로고
    • Extracellular biology of Myxococcus xanthus
    • Konovalova A, Petters T, Søgaard-Andersen L. 2010. Extracellular biology of Myxococcus xanthus. FEMS Microbiol Rev 34:89-106. http://dx.doi.org/10.1111/j.1574-6976.2009.00194.x.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 89-106
    • Konovalova, A.1    Petters, T.2    Søgaard-Andersen, L.3
  • 19
    • 79956308305 scopus 로고    scopus 로고
    • Motordriven intracellular transport powers bacterial gliding motility
    • Sun M, Wartel M, Cascales E, Shaevitz JW, Mignot T. 2011. Motordriven intracellular transport powers bacterial gliding motility. Proc Natl Acad Sci U S A 108:7559-7564. http://dx.doi.org/10.1073/pnas.1101101108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7559-7564
    • Sun, M.1    Wartel, M.2    Cascales, E.3    Shaevitz, J.W.4    Mignot, T.5
  • 20
    • 77953497996 scopus 로고    scopus 로고
    • A multi-protein complex from Myxococcus xanthus required for bacterial gliding motility
    • Nan BY, Mauriello EMF, Sun IH, Wong A, Zusman DR. 2010. A multi-protein complex from Myxococcus xanthus required for bacterial gliding motility. Mol Microbiol 76:1539-1554. http://dx.doi.org/10.1111/j.1365-2958.2010.07184.x.
    • (2010) Mol Microbiol , vol.76 , pp. 1539-1554
    • Nan, B.Y.1    Mauriello, E.M.F.2    Sun, I.H.3    Wong, A.4    Zusman, D.R.5
  • 21
    • 33846965170 scopus 로고    scopus 로고
    • Evidence that focal adhesion complexes power bacterial gliding motility
    • Mignot T, Shaevitz JW, Hartzell PL, Zusman DR. 2007. Evidence that focal adhesion complexes power bacterial gliding motility. Science 315:853-856. http://dx.doi.org/10.1126/science.1137223.
    • (2007) Science , vol.315 , pp. 853-856
    • Mignot, T.1    Shaevitz, J.W.2    Hartzell, P.L.3    Zusman, D.R.4
  • 22
    • 79952293671 scopus 로고    scopus 로고
    • Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force
    • Nan B, Chen J, Neu JC, Berry RM, Oster G, Zusman DR. 2011. Myxobacteria gliding motility requires cytoskeleton rotation powered by proton motive force. Proc Natl Acad Sci U S A 108:2498-2503. http://dx.doi.org/10.1073/pnas.1018556108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2498-2503
    • Nan, B.1    Chen, J.2    Neu, J.C.3    Berry, R.M.4    Oster, G.5    Zusman, D.R.6
  • 23
    • 84862572353 scopus 로고    scopus 로고
    • Wet-surface-enhanced ellipsometric contrast microscopy identifies slime as a major adhesion factor during bacterial surface motility
    • Ducret A, Valignat MP, Mouhamar F, Mignot T, Theodoly O. 2012. Wet-surface-enhanced ellipsometric contrast microscopy identifies slime as a major adhesion factor during bacterial surface motility. Proc Natl Acad Sci U S A 109:10036-10041. http://dx.doi.org/10.1073/pnas.1120979109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10036-10041
    • Ducret, A.1    Valignat, M.P.2    Mouhamar, F.3    Mignot, T.4    Theodoly, O.5
  • 24
    • 42649085698 scopus 로고    scopus 로고
    • Type IV pili: pluribus unum?
    • Pelicic V. 2008. Type IV pili: pluribus unum? Mol Microbiol 68:827-837. http://dx.doi.org/10.1111/j.1365-2958.2008.06197.x.
    • (2008) Mol Microbiol , vol.68 , pp. 827-837
    • Pelicic, V.1
  • 25
    • 0038302837 scopus 로고    scopus 로고
    • Extracellular polysaccharides mediate pilus retraction during social motility of Myxococcus xanthus
    • Li Y, Sun H, Ma X, Lu A, Lux R, Zusman D, Shi W. 2003. Extracellular polysaccharides mediate pilus retraction during social motility of Myxococcus xanthus. Proc Natl Acad Sci USA 100:5443-5448. http://dx.doi.org/10.1073/pnas.0836639100.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5443-5448
    • Li, Y.1    Sun, H.2    Ma, X.3    Lu, A.4    Lux, R.5    Zusman, D.6    Shi, W.7
  • 26
    • 0033808729 scopus 로고    scopus 로고
    • Myxococcus xanthus dif genes are required for biogenesis of cell surface fibrils essential for social gliding motility
    • Yang Z, Ma X, Tong L, Kaplan HB, Shimkets LJ, Shi W. 2000. Myxococcus xanthus dif genes are required for biogenesis of cell surface fibrils essential for social gliding motility. J Bacteriol 182:5793-5798. http://dx.doi.org/10.1128/JB.182.20.5793-5798.2000.
    • (2000) J Bacteriol , vol.182 , pp. 5793-5798
    • Yang, Z.1    Ma, X.2    Tong, L.3    Kaplan, H.B.4    Shimkets, L.J.5    Shi, W.6
  • 27
    • 0141960322 scopus 로고    scopus 로고
    • Global mutational analysis of NtrC-like activators in Myxococcus xanthus: identifying activator mutants defective for motility and fruiting body development
    • Caberoy NB, Welch RD, Jakobsen JS, Slater SC, Garza AG. 2003. Global mutational analysis of NtrC-like activators in Myxococcus xanthus: identifying activator mutants defective for motility and fruiting body development. J Bacteriol 185:6083-6094. http://dx.doi.org/10.1128/JB.185.20.6083-6094.2003.
    • (2003) J Bacteriol , vol.185 , pp. 6083-6094
    • Caberoy, N.B.1    Welch, R.D.2    Jakobsen, J.S.3    Slater, S.C.4    Garza, A.G.5
  • 28
    • 80051859724 scopus 로고    scopus 로고
    • FrzS regulates social motility in Myxococcus xanthus by controlling exopolysaccharide production
    • Berleman JE, Vicente JJ, Davis AE, Jiang SY, Seo Y-E, Zusman DR. 2011. FrzS regulates social motility in Myxococcus xanthus by controlling exopolysaccharide production. PLoS One 6:e23920. http://dx.doi.org/10.1371/journal.pone.0023920.
    • (2011) PLoS One , vol.6
    • Berleman, J.E.1    Vicente, J.J.2    Davis, A.E.3    Jiang, S.Y.4    Seo, Y.-E.5    Zusman, D.R.6
  • 29
    • 0036886520 scopus 로고    scopus 로고
    • MglA, a small GTPase, interacts with a tyrosine kinase to control type IV pili-mediated motility and development of Myxococcus xanthus
    • Thomasson B, Link J, Stassinopoulos AG, Burke N, Plamann L, Hartzell PL. 2002. MglA, a small GTPase, interacts with a tyrosine kinase to control type IV pili-mediated motility and development of Myxococcus xanthus. Mol Microbiol 46:1399-1413. http://dx.doi.org/10.1046/j.1365-2958.2002.03258.x.
    • (2002) Mol Microbiol , vol.46 , pp. 1399-1413
    • Thomasson, B.1    Link, J.2    Stassinopoulos, A.G.3    Burke, N.4    Plamann, L.5    Hartzell, P.L.6
  • 30
    • 19944407424 scopus 로고    scopus 로고
    • Characterization of a Myxococcus xanthus mutant that is defective for adventurous motility and social motility
    • Lancero H, Caberoy NB, Castaneda S, Li Y, Lu A, Dutton D, Duan X-Y, Kaplan HB, Shi W, Garza AG. 2004. Characterization of a Myxococcus xanthus mutant that is defective for adventurous motility and social motility. Microbiology 150:4085-4093. http://dx.doi.org/10.1099/mic.0.27381-0.
    • (2004) Microbiology , vol.150 , pp. 4085-4093
    • Lancero, H.1    Caberoy, N.B.2    Castaneda, S.3    Li, Y.4    Lu, A.5    Dutton, D.6    Duan, X.-Y.7    Kaplan, H.B.8    Shi, W.9    Garza, A.G.10
  • 31
    • 33744972113 scopus 로고    scopus 로고
    • The orphan response regulator DigR is required for synthesis of extracellular matrix fibrils in Myxococcus xanthus
    • Overgaard M, Wegener-Feldbrügge S, Søgaard-Andersen L. 2006. The orphan response regulator DigR is required for synthesis of extracellular matrix fibrils in Myxococcus xanthus. J Bacteriol 188:4384-4394. http://dx.doi.org/10.1128/JB.00189-06.
    • (2006) J Bacteriol , vol.188 , pp. 4384-4394
    • Overgaard, M.1    Wegener-Feldbrügge, S.2    Søgaard-Andersen, L.3
  • 32
    • 0031680540 scopus 로고    scopus 로고
    • A chaperone in the HSP70 family controls production of extracellular fibrils in Myxococcus xanthus
    • Weimer RM, Creighton C, Stassinopoulos A, Youderian P, Hartzell PL. 1998. A chaperone in the HSP70 family controls production of extracellular fibrils in Myxococcus xanthus. J Bacteriol 180:5357-5368.
    • (1998) J Bacteriol , vol.180 , pp. 5357-5368
    • Weimer, R.M.1    Creighton, C.2    Stassinopoulos, A.3    Youderian, P.4    Hartzell, P.L.5
  • 33
    • 0027266786 scopus 로고
    • Regulation of cohesion-dependent cell interactions in Myxococcus xanthus
    • Dana JR, Shimkets LJ. 1993. Regulation of cohesion-dependent cell interactions in Myxococcus xanthus. J Bacteriol 175:3636-3647.
    • (1993) J Bacteriol , vol.175 , pp. 3636-3647
    • Dana, J.R.1    Shimkets, L.J.2
  • 34
    • 19044397490 scopus 로고    scopus 로고
    • Analysing protein-protein interactions of the Myxococcus xanthus Dif signalling pathway using the yeast two-hybrid system
    • Lancero HL, Castaneda S, Caberoy NB, Ma X, Garza AG, Shi W. 2005. Analysing protein-protein interactions of the Myxococcus xanthus Dif signalling pathway using the yeast two-hybrid system. Microbiology 151:1535-1541. http://dx.doi.org/10.1099/mic.0.27743-0.
    • (2005) Microbiology , vol.151 , pp. 1535-1541
    • Lancero, H.L.1    Castaneda, S.2    Caberoy, N.B.3    Ma, X.4    Garza, A.G.5    Shi, W.6
  • 36
    • 0017387488 scopus 로고
    • Cell-to-cell stimulation of movement in nonmotile mutants of Myxococcus
    • Hodgkin J, Kaiser D. 1977. Cell-to-cell stimulation of movement in nonmotile mutants of Myxococcus. Proc Natl Acad Sci U S A 74:2938-2942. http://dx.doi.org/10.1073/pnas.74.7.2938.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 2938-2942
    • Hodgkin, J.1    Kaiser, D.2
  • 37
    • 0018536781 scopus 로고
    • Social gliding is correlated with the presence of pili in Myxococcus xanthus
    • Kaiser D. 1979. Social gliding is correlated with the presence of pili in Myxococcus xanthus. Proc Natl Acad Sci U S A 76:5952-5956. http://dx.doi.org/10.1073/pnas.76.11.5952.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 5952-5956
    • Kaiser, D.1
  • 38
    • 38749132556 scopus 로고    scopus 로고
    • Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus
    • Shi X, Wegener-Feldbrugge S, Huntley S, Hamann N, Hedderich R, Søgaard-Andersen L. 2008. Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus. J Bacteriol 190:613-624. http://dx.doi.org/10.1128/JB.01502-07.
    • (2008) J Bacteriol , vol.190 , pp. 613-624
    • Shi, X.1    Wegener-Feldbrugge, S.2    Huntley, S.3    Hamann, N.4    Hedderich, R.5    Søgaard-Andersen, L.6
  • 39
    • 0003903343 scopus 로고    scopus 로고
    • Molecular cloning: a laboratory manual
    • 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 40
    • 1142286468 scopus 로고    scopus 로고
    • Myxococcus xanthus chemotaxis homologs DifD and DifG negatively regulate fibril polysaccharide production
    • Black WP, Yang Z. 2004. Myxococcus xanthus chemotaxis homologs DifD and DifG negatively regulate fibril polysaccharide production. J Bacteriol 186:1001-1008. http://dx.doi.org/10.1128/JB.186.4.1001-1008.2004.
    • (2004) J Bacteriol , vol.186 , pp. 1001-1008
    • Black, W.P.1    Yang, Z.2
  • 41
    • 0022642970 scopus 로고
    • Correlation of energy-dependent cell cohesion with social motility in Myxococcus xanthus
    • Shimkets LJ. 1986. Correlation of energy-dependent cell cohesion with social motility in Myxococcus xanthus. J Bacteriol 166:837-841.
    • (1986) J Bacteriol , vol.166 , pp. 837-841
    • Shimkets, L.J.1
  • 42
    • 15644383107 scopus 로고    scopus 로고
    • Regulation of expression of the pilA gene in Myxococcus xanthus
    • Wu SS, Kaiser D. 1997. Regulation of expression of the pilA gene in Myxococcus xanthus. J Bacteriol 179:7748-7758.
    • (1997) J Bacteriol , vol.179 , pp. 7748-7758
    • Wu, S.S.1    Kaiser, D.2
  • 44
    • 41549119041 scopus 로고    scopus 로고
    • PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus
    • Jakovljevic V, Leonardy S, Hoppert M, Søgaard-Andersen L. 2008. PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus. J Bacteriol 190:2411-2421. http://dx.doi.org/10.1128/JB.01793-07.
    • (2008) J Bacteriol , vol.190 , pp. 2411-2421
    • Jakovljevic, V.1    Leonardy, S.2    Hoppert, M.3    Søgaard-Andersen, L.4
  • 45
    • 77952580705 scopus 로고    scopus 로고
    • A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate
    • Spangler C, Bohm A, Jenal U, Seifert R, Kaever V. 2010. A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate. J Microbiol Methods 81:226-231. http://dx.doi.org/10.1016/j.mimet.2010.03.020.
    • (2010) J Microbiol Methods , vol.81 , pp. 226-231
    • Spangler, C.1    Bohm, A.2    Jenal, U.3    Seifert, R.4    Kaever, V.5
  • 46
    • 77649166010 scopus 로고    scopus 로고
    • Beyond antibiotic resistance: integrating conjugative elements of the SXT/R391 family that encode novel diguanylate cyclases participate to c-di-GMP signalling in Vibrio cholerae
    • Bordeleau E, Brouillette E, Robichaud N, Burrus V. 2010. Beyond antibiotic resistance: integrating conjugative elements of the SXT/R391 family that encode novel diguanylate cyclases participate to c-di-GMP signalling in Vibrio cholerae. Environ Microbiol 12:510-523. http://dx.doi.org/10.1111/j.1462-2920.2009.02094.x.
    • (2010) Environ Microbiol , vol.12 , pp. 510-523
    • Bordeleau, E.1    Brouillette, E.2    Robichaud, N.3    Burrus, V.4
  • 47
    • 79961113805 scopus 로고    scopus 로고
    • Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi
    • Sultan SZ, Pitzer JE, Boquoi T, Hobbs G, Miller MR, Motaleb MA. 2011. Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi. Infect Immun 79:3273-3283. http://dx.doi.org/10.1128/IAI.05153-11.
    • (2011) Infect Immun , vol.79 , pp. 3273-3283
    • Sultan, S.Z.1    Pitzer, J.E.2    Boquoi, T.3    Hobbs, G.4    Miller, M.R.5    Motaleb, M.A.6
  • 48
    • 80053091424 scopus 로고    scopus 로고
    • Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions
    • Roelofs KG, Wang J, Sintim HO, Lee VT. 2011. Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions. Proc Natl Acad Sci U S A 108:15528-15533. http://dx.doi.org/10.1073/pnas.1018949108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15528-15533
    • Roelofs, K.G.1    Wang, J.2    Sintim, H.O.3    Lee, V.T.4
  • 49
    • 84904859048 scopus 로고    scopus 로고
    • GIL, a new c-di-GMP-binding protein domain involved in regulation of cellulose synthesis in enterobacteria
    • Fang X, Ahmad I, Blanka A, Schottkowski M, Cimdins A, Galperin MY, Romling U, Gomelsky M. 2014. GIL, a new c-di-GMP-binding protein domain involved in regulation of cellulose synthesis in enterobacteria. Mol Microbiol 93:439-452. http://dx.doi.org/10.1111/mmi.12672.
    • (2014) Mol Microbiol , vol.93 , pp. 439-452
    • Fang, X.1    Ahmad, I.2    Blanka, A.3    Schottkowski, M.4    Cimdins, A.5    Galperin, M.Y.6    Romling, U.7    Gomelsky, M.8
  • 50
    • 33645213032 scopus 로고    scopus 로고
    • Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP
    • Thormann KM, Duttler S, Saville RM, Hyodo M, Shukla S, Hayakawa Y, Spormann AM. 2006. Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP. J Bacteriol 188:2681-2691. http://dx.doi.org/10.1128/JB.188.7.2681-2691.2006.
    • (2006) J Bacteriol , vol.188 , pp. 2681-2691
    • Thormann, K.M.1    Duttler, S.2    Saville, R.M.3    Hyodo, M.4    Shukla, S.5    Hayakawa, Y.6    Spormann, A.M.7
  • 51
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • Tischler AD, Camilli A. 2004. Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol Microbiol 53:857-869. http://dx.doi.org/10.1111/j.1365-2958.2004.04155.x.
    • (2004) Mol Microbiol , vol.53 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 52
    • 79955085332 scopus 로고    scopus 로고
    • Cyclic diguanylate signaling proteins control intracellular growth of Legionella pneumophila
    • Levi A, Folcher M, Jenal U, Shuman HA. 2011. Cyclic diguanylate signaling proteins control intracellular growth of Legionella pneumophila. mBio 2:e00316-10. http://dx.doi.org/10.1128/mBio.00316-10.
    • (2011) mBio , vol.2 , pp. e00316-e00410
    • Levi, A.1    Folcher, M.2    Jenal, U.3    Shuman, H.A.4
  • 55
    • 33747080072 scopus 로고    scopus 로고
    • Type IV pili function upstream of the Dif chemotaxis pathway in Myxococcus xanthus EPS regulation
    • Black WP, Xu Q, Yang Z. 2006. Type IV pili function upstream of the Dif chemotaxis pathway in Myxococcus xanthus EPS regulation. Mol Microbiol 61:447-456. http://dx.doi.org/10.1111/j.1365-2958.2006.05230.x.
    • (2006) Mol Microbiol , vol.61 , pp. 447-456
    • Black, W.P.1    Xu, Q.2    Yang, Z.3
  • 56
    • 0024258226 scopus 로고
    • Cell surface properties correlated with cohesion in Myxococcus xanthus
    • Arnold JW, Shimkets LJ. 1988. Cell surface properties correlated with cohesion in Myxococcus xanthus. J Bacteriol 170:5771-5777.
    • (1988) J Bacteriol , vol.170 , pp. 5771-5777
    • Arnold, J.W.1    Shimkets, L.J.2
  • 57
    • 0035007193 scopus 로고    scopus 로고
    • The act operon controls the level and time of C-signal production for Myxococcus xanthus development
    • Gronewold TM, Kaiser D. 2001. The act operon controls the level and time of C-signal production for Myxococcus xanthus development. Mol Microbiol 40:744-756. http://dx.doi.org/10.1046/j.1365-2958.2001.02428.x.
    • (2001) Mol Microbiol , vol.40 , pp. 744-756
    • Gronewold, T.M.1    Kaiser, D.2
  • 59
    • 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. http://dx.doi.org/10.1074/jbc.M704702200.
    • (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
  • 60
    • 0022652264 scopus 로고
    • Role of cell cohesion in Myxococcus xanthus fruiting body formation
    • Shimkets LJ. 1986. Role of cell cohesion in Myxococcus xanthus fruiting body formation. J Bacteriol 166:842-848.
    • (1986) J Bacteriol , vol.166 , pp. 842-848
    • Shimkets, L.J.1
  • 61
    • 76749083886 scopus 로고    scopus 로고
    • Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP
    • Krasteva PV, Fong JC, Shikuma NJ, Beyhan S, Navarro MV, Yildiz FH, Sondermann H. 2010. Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science 327:866-868. http://dx.doi.org/10.1126/science.1181185.
    • (2010) Science , vol.327 , pp. 866-868
    • Krasteva, P.V.1    Fong, J.C.2    Shikuma, N.J.3    Beyhan, S.4    Navarro, M.V.5    Yildiz, F.H.6    Sondermann, H.7
  • 62
    • 80655125443 scopus 로고    scopus 로고
    • Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae
    • Srivastava D, Harris RC, Waters CM. 2011. Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae. J Bacteriol 193:6331-6341. http://dx.doi.org/10.1128/JB.05167-11.
    • (2011) J Bacteriol , vol.193 , pp. 6331-6341
    • Srivastava, D.1    Harris, R.C.2    Waters, C.M.3
  • 63
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman JW, Harwood CS. 2008. Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol Microbiol 69:376-389. http://dx.doi.org/10.1111/j.1365-2958.2008.06281.x.
    • (2008) Mol Microbiol , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 64
    • 77950370030 scopus 로고    scopus 로고
    • The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism
    • Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM. 2010. The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol Cell 38:128-139. http://dx.doi.org/10.1016/j.molcel.2010.03.001.
    • (2010) Mol Cell , vol.38 , pp. 128-139
    • Paul, K.1    Nieto, V.2    Carlquist, W.C.3    Blair, D.F.4    Harshey, R.M.5
  • 67
    • 33646397872 scopus 로고    scopus 로고
    • Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
    • Kazmierczak BI, Lebron MB, Murray TS. 2006. Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Mol Microbiol 60:1026-1043. http://dx.doi.org/10.1111/j.1365-2958.2006.05156.x.
    • (2006) Mol Microbiol , vol.60 , pp. 1026-1043
    • Kazmierczak, B.I.1    Lebron, M.B.2    Murray, T.S.3
  • 68
    • 84878261687 scopus 로고    scopus 로고
    • Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis
    • Guzzo CR, Dunger G, Salinas RK, Farah CS. 2013. Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis. J Mol Biol 425:2174-2197. http://dx.doi.org/10.1016/j.jmb.2013.03.021.
    • (2013) J Mol Biol , vol.425 , pp. 2174-2197
    • Guzzo, C.R.1    Dunger, G.2    Salinas, R.K.3    Farah, C.S.4
  • 69
    • 70349968208 scopus 로고    scopus 로고
    • PilZ protein structure and interactions with PilB and the FimX EAL domain: implicactions for control of type IV pilus biogenesis
    • Guzzo CR, Salinas RK, Andrade MO, Farah CS. 2009. PilZ protein structure and interactions with PilB and the FimX EAL domain: implicactions for control of type IV pilus biogenesis. J Mol Biol 393:848-866. http://dx.doi.org/10.1016/j.jmb.2009.07.065.
    • (2009) J Mol Biol , vol.393 , pp. 848-866
    • Guzzo, C.R.1    Salinas, R.K.2    Andrade, M.O.3    Farah, C.S.4
  • 70
    • 84946060416 scopus 로고    scopus 로고
    • SMART: recent updates, new developments and status in 2015
    • Letunic I, Doerks T, Bork P. 2015. SMART: recent updates, new developments and status in 2015. Nucleic Acids Res 43:D257-D260. http://dx.doi.org/10.1093/nar/gku949.
    • (2015) Nucleic Acids Res , vol.43 , pp. D257-D260
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 71
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T. 2007. Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15:915-927. http://dx.doi.org/10.1016/j.str.2007.06.016.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6    Schirmer, T.7
  • 72
    • 84865519312 scopus 로고    scopus 로고
    • Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product
    • Vorobiev S, Neely H, Yu B, Seetharaman J, Xiao R, Acton T, Montelione G, Hunt J. 2012. Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product. J Struct Funct Genomics 13:177-183. http://dx.doi.org/10.1007/s10969-012-9136-4.
    • (2012) J Struct Funct Genomics , vol.13 , pp. 177-183
    • Vorobiev, S.1    Neely, H.2    Yu, B.3    Seetharaman, J.4    Xiao, R.5    Acton, T.6    Montelione, G.7    Hunt, J.8
  • 73
    • 67649746308 scopus 로고    scopus 로고
    • Crystal structures of YkuI and its complex with second messenger cyclic di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains
    • Minasov G, Padavattan S, Shuvalova L, Brunzelle JS, Miller DJ, Baslé A, Massa C, Collart FR, Schirmer T, Anderson WF. 2009. Crystal structures of YkuI and its complex with second messenger cyclic di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains. J Biol Chem 284:13174-13184. http://dx.doi.org/10.1074/jbc.M808221200.
    • (2009) J Biol Chem , vol.284 , pp. 13174-13184
    • Minasov, G.1    Padavattan, S.2    Shuvalova, L.3    Brunzelle, J.S.4    Miller, D.J.5    Baslé, A.6    Massa, C.7    Collart, F.R.8    Schirmer, T.9    Anderson, W.F.10
  • 74
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao F, Yang Y, Qi Y, Liang Z-X. 2008. Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J Bacteriol 190:3622-3631. http://dx.doi.org/10.1128/JB.00165-08.
    • (2008) J Bacteriol , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.-X.4
  • 75
    • 84891143422 scopus 로고    scopus 로고
    • Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre
    • Bellini D, Caly DL, McCarthy Y, Bumann M, An S-Q, Dow JM, Ryan RP, Walsh MA. 2014. Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. Mol Microbiol 91:26-38. http://dx.doi.org/10.1111/mmi.12447.
    • (2014) Mol Microbiol , vol.91 , pp. 26-38
    • Bellini, D.1    Caly, D.L.2    McCarthy, Y.3    Bumann, M.4    An, S.-Q.5    Dow, J.M.6    Ryan, R.P.7    Walsh, M.A.8
  • 76
    • 80455158430 scopus 로고    scopus 로고
    • The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases
    • Lovering AL, Capeness MJ, Lambert C, Hobley L, Sockett RE. 2011. The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases. mBio 2:e00163-11. http://dx.doi.org/10.1128/mBio.00163-11.
    • (2011) mBio , vol.2 , pp. e00163-e00211
    • Lovering, A.L.1    Capeness, M.J.2    Lambert, C.3    Hobley, L.4    Sockett, R.E.5
  • 77
    • 84861918212 scopus 로고    scopus 로고
    • A full-length bifunctional protein involved in c-di-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis
    • Bharati BK, Sharma IM, Kasetty S, Kumar M, Mukherjee R, Chatterji D. 2012. A full-length bifunctional protein involved in c-di-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis. Microbiology 158:1415-1427. http://dx.doi.org/10.1099/mic.0.053892-0.
    • (2012) Microbiology , vol.158 , pp. 1415-1427
    • Bharati, B.K.1    Sharma, I.M.2    Kasetty, S.3    Kumar, M.4    Mukherjee, R.5    Chatterji, D.6
  • 78
    • 0018293841 scopus 로고
    • Genetics of gliding motility in Myxococcus xanthus (Myxobacterales): two gene systems control movement
    • Hodgkin J, Kaiser D. 1979. Genetics of gliding motility in Myxococcus xanthus (Myxobacterales): two gene systems control movement. Mol Gen Genet 171:177-191. http://dx.doi.org/10.1007/BF00270004.
    • (1979) Mol Gen Genet , vol.171 , pp. 177-191
    • Hodgkin, J.1    Kaiser, D.2
  • 79
    • 0031767106 scopus 로고    scopus 로고
    • A new set of chemotaxis homologues is essential for Myxococcus xanthus social motility
    • Yang Z, Geng Y, Xu D, Kaplan HB, Shi W. 1998. A new set of chemotaxis homologues is essential for Myxococcus xanthus social motility. Mol Microbiol 30:1123-1130. http://dx.doi.org/10.1046/j.1365-2958.1998.01160.x.
    • (1998) Mol Microbiol , vol.30 , pp. 1123-1130
    • Yang, Z.1    Geng, Y.2    Xu, D.3    Kaplan, H.B.4    Shi, W.5
  • 80
    • 0029796393 scopus 로고    scopus 로고
    • Markerless deletions of pil genes in Myxococcus xanthus generated by counterselection with the Bacillus subtilis sacB gene
    • Wu SS, Kaiser D. 1996. Markerless deletions of pil genes in Myxococcus xanthus generated by counterselection with the Bacillus subtilis sacB gene. J Bacteriol 178:5817-5821.
    • (1996) J Bacteriol , vol.178 , pp. 5817-5821
    • Wu, S.S.1    Kaiser, D.2
  • 81
    • 0034255140 scopus 로고    scopus 로고
    • Spatial control of cell differentiation in Myxococcus xanthus
    • Julien B, Kaiser AD, Garza A. 2000. Spatial control of cell differentiation in Myxococcus xanthus. Proc Natl Acad Sci USA 97:9098-9103. http://dx.doi.org/10.1073/pnas.97.16.9098.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9098-9103
    • Julien, B.1    Kaiser, A.D.2    Garza, A.3
  • 82
    • 0022495405 scopus 로고
    • Kanamycin-resistant vectors that are analogues of plasmids pUC8, pUC9, pEMBL8 and pEMBL9
    • Spratt BG, Hedge PJ, Ste Heesen Edelman A, Broome-Smith JK. 1986. Kanamycin-resistant vectors that are analogues of plasmids pUC8, pUC9, pEMBL8 and pEMBL9. Gene 41:337-342. http://dx.doi.org/10.1016/0378-1119(86)90117-4.
    • (1986) Gene , vol.41 , pp. 337-342
    • Spratt, B.G.1    Hedge, P.J.2    Ste Heesen Edelman, A.3    Broome-Smith, J.K.4

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.