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Volumn 194, Issue 17, 2012, Pages 4642-4651

Cyclic Di-GMP phosphodiesterases RmdA and RmdB are involved in regulating colony morphology and development in Streptomyces coelicolor

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC GMP PHOSPHODIESTERASE; RMDA PROTEIN; RMDB PROTEIN; UNCLASSIFIED DRUG;

EID: 84866330705     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00157-12     Document Type: Article
Times cited : (36)

References (65)
  • 1
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam D, Galperin MY. 2006. PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22:3-6.
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 2
    • 79960021998 scopus 로고    scopus 로고
    • Improved poly-epsilon-lysine biosynthesis using Streptomyces noursei NRRL 5126 by controlling dissolved oxygen during fermentation
    • Bankar SB, Singhal RS. 2011. Improved poly-epsilon-lysine biosynthesis using Streptomyces noursei NRRL 5126 by controlling dissolved oxygen during fermentation. J. Microbiol. Biotechnol. 21:652-658.
    • (2011) J. Microbiol. Biotechnol. , vol.21 , pp. 652-658
    • Bankar, S.B.1    Singhal, R.S.2
  • 3
    • 67649295467 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial lightregulated cyclic nucleotide phosphodiesterase
    • Barends TR, et al. 2009. Structure and mechanism of a bacterial lightregulated cyclic nucleotide phosphodiesterase. Nature 459:1015-1018.
    • (2009) Nature , vol.459 , pp. 1015-1018
    • Barends, T.R.1
  • 4
    • 58649090937 scopus 로고    scopus 로고
    • Molecular genetic analysis of division and development in Streptomyces coelicolor
    • Duquesne University, Pittsburgh, PA
    • Bennett JA. 2007. Molecular genetic analysis of division and development in Streptomyces coelicolor. Ph.D. dissertation. Duquesne University, Pittsburgh, PA.
    • (2007) Ph.D. dissertation
    • Bennett, J.A.1
  • 5
    • 0035928766 scopus 로고    scopus 로고
    • Two new loci affecting cell division identified as suppressors of an ftsQ-null mutation in Streptomyces coelicolor A3(2)
    • Bennett JA, McCormick JR. 2001. Two new loci affecting cell division identified as suppressors of an ftsQ-null mutation in Streptomyces coelicolor A3(2). FEMS Microbiol. Lett. 202:251-256.
    • (2001) FEMS Microbiol. Lett. , vol.202 , pp. 251-256
    • Bennett, J.A.1    Mccormick, J.R.2
  • 6
    • 0037046560 scopus 로고    scopus 로고
    • Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
    • Bentley SD, et al. 2002. Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417:141-147.
    • (2002) Nature , vol.417 , pp. 141-147
    • Bentley, S.D.1
  • 7
    • 2442715070 scopus 로고    scopus 로고
    • Systematic insertional mutagenesis of a streptomycete genome: a link between osmoadaptation and antibiotic production
    • Bishop A, Fielding S, Dyson P, Herron P. 2004. Systematic insertional mutagenesis of a streptomycete genome: a link between osmoadaptation and antibiotic production. Genome Res. 14:893-900.
    • (2004) Genome Res. , vol.14 , pp. 893-900
    • Bishop, A.1    Fielding, S.2    Dyson, P.3    Herron, P.4
  • 8
    • 78651109050 scopus 로고    scopus 로고
    • Systematic analysis of cyclic di-GMP signalling enzymes and their role in biofilm formation and virulence in Yersinia pestis
    • Bobrov AG, et al. 2011. Systematic analysis of cyclic di-GMP signalling enzymes and their role in biofilm formation and virulence in Yersinia pestis. Mol. Microbiol. 79:533-551.
    • (2011) Mol. Microbiol. , vol.79 , pp. 533-551
    • Bobrov, A.G.1
  • 9
    • 79953733174 scopus 로고    scopus 로고
    • c-di-GMP turnover in Clostridium difficile is controlled by a plethora of diguanylate cyclases and phosphodiesterases
    • doi:10.1371/journal.pgen.1002039
    • Bordeleau E, Fortier LC, Malouin F, Burrus V. 2011. c-di-GMP turnover in Clostridium difficile is controlled by a plethora of diguanylate cyclases and phosphodiesterases. PLoS Genet. 7:e1002039. doi:10.1371/journal.pgen.1002039.
    • (2011) PLoS Genet. , vol.7
    • Bordeleau, E.1    Fortier, L.C.2    Malouin, F.3    Burrus, V.4
  • 10
    • 34247492536 scopus 로고    scopus 로고
    • SapB and the chaplins: connections between morphogenetic proteins in Streptomyces coelicolor
    • Capstick DS, Willey JM, Buttner MJ, Elliot MA. 2007. SapB and the chaplins: connections between morphogenetic proteins in Streptomyces coelicolor. Mol. Microbiol. 64:602-613.
    • (2007) Mol. Microbiol. , vol.64 , pp. 602-613
    • Capstick, D.S.1    Willey, J.M.2    Buttner, M.J.3    Elliot, M.A.4
  • 11
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • U.S.A
    • Chan C, et al. 2004. Structural basis of activity and allosteric control of diguanylate cyclase. Proc. Natl. Acad. Sci. U. S. A. 101:17084-17089.
    • (2004) Proc. Natl. Acad. Sci. , vol.101
    • Chan, C.1
  • 12
    • 0035957226 scopus 로고    scopus 로고
    • Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor
    • Chang AL, et al. 2001. Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor. Biochemistry 40:3420-3426.
    • (2001) Biochemistry , vol.40 , pp. 3420-3426
    • Chang, A.L.1
  • 13
    • 0002375902 scopus 로고    scopus 로고
    • Developmental decisions during sporulation in the aerial mycelium in Streptomyces
    • ASM Press, Washington, DC. In Brun YV, Shimkets LJ (ed)
    • Chater KF. 2000. Developmental decisions during sporulation in the aerial mycelium in Streptomyces, p 33-48. In Brun YV, Shimkets LJ (ed), Prokaryotic development. ASM Press, Washington, DC.
    • (2000) Prokaryotic development , pp. 33-48
    • Chater, K.F.1
  • 14
    • 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
  • 15
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
    • Claessen D, et al. 2003. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev. 17:1714-1726.
    • (2003) Genes Dev. , vol.17 , pp. 1714-1726
    • Claessen, D.1
  • 16
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon VM, Gonzalez G, Gilles-Gonzalez MA. 2000. Dos, a heme-binding PAS 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
  • 17
    • 78649368524 scopus 로고    scopus 로고
    • Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth
    • den Hengst CD, et al. 2010. Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth. Mol. Microbiol. 78:361-379.
    • (2010) Mol. Microbiol. , vol.78 , pp. 361-379
    • Hengst, C.D.D.1
  • 18
    • 0038681008 scopus 로고    scopus 로고
    • The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor
    • Elliot MA, et al. 2003. The chaplins: a family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor. Genes Dev. 17:1727-1740.
    • (2003) Genes Dev. , vol.17 , pp. 1727-1740
    • Elliot, M.A.1
  • 19
    • 77952813357 scopus 로고    scopus 로고
    • A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility
    • Fang X, Gomelsky M. 2010. A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility. Mol. Microbiol. 76:1295-1305.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1295-1305
    • Fang, X.1    Gomelsky, M.2
  • 20
    • 38649102818 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus ScrC modulates cyclic dimeric GMP regulation of gene expression relevant to growth on surfaces
    • Ferreira RB, Antunes LC, Greenberg EP, McCarter LL. 2008. Vibrio parahaemolyticus ScrC modulates cyclic dimeric GMP regulation of gene expression relevant to growth on surfaces. J. Bacteriol. 190:851-860.
    • (2008) J. Bacteriol. , vol.190 , pp. 851-860
    • Ferreira, R.B.1    Antunes, L.C.2    Greenberg, E.P.3    Mccarter, L.L.4
  • 21
    • 75549090603 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Finn RD, et al. 2010. The Pfam protein families database. Nucleic Acids Res. 38:D211-D222.
    • (2010) Nucleic Acids Res. , vol.38
    • Finn, R.D.1
  • 22
    • 55549086417 scopus 로고    scopus 로고
    • Streptomyces morphogenetics: dissecting differentiation in a filamentous bacterium
    • Flardh K, Buttner MJ. 2009. Streptomyces morphogenetics: dissecting differentiation in a filamentous bacterium. Nat. Rev. Microbiol. 7:36-49.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 36-49
    • Flardh, K.1    Buttner, M.J.2
  • 24
    • 0032567446 scopus 로고    scopus 로고
    • AppA, a redox regulator of photosystem formation in Rhodobacter sphaeroides 2.4.1, is a flavoprotein. Identification of a novel fad binding domain
    • Gomelsky M, Kaplan S. 1998. AppA, a redox regulator of photosystem formation in Rhodobacter sphaeroides 2.4.1, is a flavoprotein. Identification of a novel fad binding domain. J. Biol. Chem. 273:35319-35325.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35319-35325
    • Gomelsky, M.1    Kaplan, S.2
  • 25
    • 0032438105 scopus 로고    scopus 로고
    • Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction
    • U.S.A
    • Gong W, et al. 1998. Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc. Natl. Acad. Sci. U. S. A. 95:15177-15182.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15177-15182
    • Gong, W.1
  • 26
    • 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.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 263-273
    • Hengge, R.1
  • 27
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • Henry JT, Crosson S. 2011. Ligand-binding PAS domains in a genomic, cellular, and structural context. Annu. Rev. Microbiol. 65:261-286.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 28
    • 84860905515 scopus 로고    scopus 로고
    • Discrete cyclic di-GMP-dependent control of bacterial predation versus axenic growth in Bdellovibrio bacteriovorus
    • doi:10.1371/journal.ppat.1002493
    • Hobley L, et al. 2012. Discrete cyclic di-GMP-dependent control of bacterial predation versus axenic growth in Bdellovibrio bacteriovorus. PLoS Pathog. 8:e1002493. doi:10.1371/journal.ppat.1002493.
    • (2012) PLoS Pathog. , vol.8
    • Hobley, L.1
  • 29
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bj- FixLH reveal details of ligand recognition and signaling
    • Key J, Moffat K. 2005. Crystal structures of deoxy and CO-bound bj- FixLH reveal details of ligand recognition and signaling. Biochemistry 44:4627-4635.
    • (2005) Biochemistry , vol.44 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 31
    • 3843091511 scopus 로고    scopus 로고
    • The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor
    • U.S.A
    • Kodani S, et al. 2004. The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor. Proc. Natl. Acad. Sci. U. S. A. 101:11448-11453.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 11448-11453
    • Kodani, S.1
  • 32
    • 55549144752 scopus 로고    scopus 로고
    • Cyclic di-GMP: a second messenger required for long-term survival, but not for biofilm formation, in Mycobacterium smegmatis
    • Kumar M, Chatterji D. 2008. Cyclic di-GMP: a second messenger required for long-term survival, but not for biofilm formation, in Mycobacterium smegmatis. Microbiology 154:2942-2955.
    • (2008) Microbiology , vol.154 , pp. 2942-2955
    • Kumar, M.1    Chatterji, D.2
  • 33
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: recent updates to the protein domain annotation resource
    • Letunic I, Doerks T, Bork P. 2012. SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40:D302-D305.
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 34
    • 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
    • doi:10.1128/mBio.00163-11
    • 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(5):e00163-11. doi:10.1128/mBio. 00163-11.
    • (2011) mBio , vol.2 , Issue.5
    • Lovering, A.L.1    Capeness, M.J.2    Lambert, C.3    Hobley, L.4    Sockett, R.E.5
  • 35
    • 0024225034 scopus 로고
    • Characterization of a unique methyl-specific restriction system in Streptomyces avermitilis
    • MacNeil DJ. 1988. Characterization of a unique methyl-specific restriction system in Streptomyces avermitilis. J. Bacteriol. 170:5607-5612.
    • (1988) J. Bacteriol. , vol.170 , pp. 5607-5612
    • Macneil, D.J.1
  • 36
    • 0029829906 scopus 로고    scopus 로고
    • Cell division gene ftsQ is required for efficient sporulation but not growth and viability in Streptomyces coelicolor A3(2)
    • McCormick JR, Losick R. 1996. Cell division gene ftsQ is required for efficient sporulation but not growth and viability in Streptomyces coelicolor A3(2). J. Bacteriol. 178:5295-5301.
    • (1996) J. Bacteriol. , vol.178 , pp. 5295-5301
    • Mccormick, J.R.1    Losick, R.2
  • 37
    • 79960463507 scopus 로고    scopus 로고
    • Oxygen supply controls the onset of pristinamycins production by Streptomyces pristinaespiralis in shaking flasks
    • Mehmood N, et al. 2011. Oxygen supply controls the onset of pristinamycins production by Streptomyces pristinaespiralis in shaking flasks. Biotechnol. Bioeng. 108:2151-2161.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 2151-2161
    • Mehmood, N.1
  • 38
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: mechanisms of signalling
    • Mills E, Pultz IS, Kulasekara HD, Miller SI. 2011. The bacterial second messenger c-di-GMP: mechanisms of signalling. Cell. Microbiol. 13:1122-1129.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1122-1129
    • Mills, E.1    Pultz, I.S.2    Kulasekara, H.D.3    Miller, S.I.4
  • 39
  • 40
    • 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
    • U.S.A
    • 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.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'toole, G.A.3
  • 41
    • 15644367785 scopus 로고    scopus 로고
    • Denaturation of circular or linear DNA facilitates targeted integrative transformation of Streptomyces coelicolor A3(2): possible relevance to other organisms
    • Oh SH, Chater KF. 1997. Denaturation of circular or linear DNA facilitates targeted integrative transformation of Streptomyces coelicolor A3(2): possible relevance to other organisms. J. Bacteriol. 179:122-127.
    • (1997) J. Bacteriol. , vol.179 , pp. 122-127
    • Oh, S.H.1    Chater, K.F.2
  • 42
    • 0032898961 scopus 로고    scopus 로고
    • Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2)
    • Paget MS, Chamberlin L, Atrih A, Foster SJ, Buttner MJ. 1999. Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2). J. Bacteriol. 181:204-211.
    • (1999) J. Bacteriol. , vol.181 , pp. 204-211
    • Paget, M.S.1    Chamberlin, L.2    Atrih, A.3    Foster, S.J.4    Buttner, M.J.5
  • 43
    • 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, et al. 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
  • 44
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8MbStreptomyces coelicolor A3(2) chromosome
    • Redenbach M, et al. 1996. A set of ordered cosmids and a detailed genetic and physical map for the 8MbStreptomyces coelicolor A3(2) chromosome. Mol. Microbiol. 21:77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1
  • 45
    • 67651215871 scopus 로고    scopus 로고
    • Prevailing concepts of c-di-GMP signaling
    • Romling U, Simm R. 2009. Prevailing concepts of c-di-GMP signaling. Contrib. Microbiol. 16:161-181.
    • (2009) Contrib. Microbiol. , vol.16 , pp. 161-181
    • Romling, U.1    Simm, R.2
  • 46
    • 0025116425 scopus 로고
    • Chemical synthesis and biological activity of cyclic nucleotide dimer, trimer, and phosphothioate derivatives
    • The cyclic diguanylic acid regulatory system of cellulose synthesis in Acetobacter xylinum
    • Ross P, et al. 1990. The cyclic diguanylic acid regulatory system of cellulose synthesis in Acetobacter xylinum. Chemical synthesis and biological activity of cyclic nucleotide dimer, trimer, and phosphothioate derivatives. J. Biol. Chem. 265:18933-18943.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18933-18943
    • Ross, P.1
  • 47
    • 0023090935 scopus 로고
    • Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid
    • Ross P, et al. 1987. Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid. Nature 325:279-281.
    • (1987) Nature , vol.325 , pp. 279-281
    • Ross, P.1
  • 48
    • 78249278151 scopus 로고    scopus 로고
    • Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction in Xanthomonas campestris
    • Ryan RP, Dow JM. 2010. Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction in Xanthomonas campestris. Virulence 1:404-408.
    • (2010) Virulence , vol.1 , pp. 404-408
    • Ryan, R.P.1    Dow, J.M.2
  • 49
    • 33646249963 scopus 로고    scopus 로고
    • Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover
    • Ryan RP, et al. 2006. Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover. Proc. Natl. Acad. Sci. U. S. A. 103:6712-6717.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6712-6717
    • Ryan, R.P.1
  • 50
    • 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 DA, Simm R, Romling 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    Romling, U.3    Gomelsky, M.4
  • 51
    • 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.
    • (2005) J. Bacteriol. , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 52
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer T, 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
  • 53
    • 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.
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 54
    • 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, et al. 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
  • 55
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo R, Pratt JT, Camilli A. 2007. Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu. Rev. Microbiol. 61:131-148.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 56
    • 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.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33324-33330
    • Tamayo, R.1    Tischler, A.D.2    Camilli, A.3
  • 57
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP
    • Tarutina M, Ryjenkov DA, Gomelsky M. 2006. An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP. J. Biol. Chem. 281:34751-34758.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 58
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB. 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
  • 59
    • 79958062471 scopus 로고    scopus 로고
    • Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor
    • Tran NT, Den Hengst CD, Gomez-Escribano JP, Buttner MJ. 2011. Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor. J. Bacteriol. 193:3100-3108.
    • (2011) J. Bacteriol. , vol.193 , pp. 3100-3108
    • Tran, N.T.1    Hengst, C.D.D.2    Gomez-Escribano, J.P.3    Buttner, M.J.4
  • 60
    • 81055141478 scopus 로고    scopus 로고
    • Bis-(3'-5')-cyclic dimeric GMP-linked quorum sensing controls swarming in Vibrio parahaemolyticus
    • U.S.A
    • Trimble MJ, McCarter LL. 2011. Bis-(3'-5')-cyclic dimeric GMP-linked quorum sensing controls swarming in Vibrio parahaemolyticus. Proc. Natl. Acad. Sci. U. S. A. 108:18079-18084.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 18079-18084
    • Trimble, M.J.1    Mccarter, L.L.2
  • 61
    • 79952735655 scopus 로고    scopus 로고
    • Cyclic di-GMP activation of polynucleotide phosphorylase signal-dependent RNA processing
    • Tuckerman JR, Gonzalez G, Gilles-Gonzalez MA. 2011. Cyclic di-GMP activation of polynucleotide phosphorylase signal-dependent RNA processing. J. Mol. Biol. 407:633-639.
    • (2011) J. Mol. Biol. , vol.407 , pp. 633-639
    • Tuckerman, J.R.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 62
    • 70350047301 scopus 로고    scopus 로고
    • An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
    • Tuckerman JR, et al. 2009. An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 48:9764-9774.
    • (2009) Biochemistry , vol.48 , pp. 9764-9774
    • Tuckerman, J.R.1
  • 63
    • 64449088389 scopus 로고    scopus 로고
    • Globins synthesize the second messenger bis-(3'-5')- cyclic diguanosine monophosphate in bacteria
    • Wan X, et al. 2009. Globins synthesize the second messenger bis-(3'-5')- cyclic diguanosine monophosphate in bacteria. J. Mol. Biol. 388:262-270.
    • (2009) J. Mol. Biol. , vol.388 , pp. 262-270
    • Wan, X.1
  • 64
    • 78650714710 scopus 로고    scopus 로고
    • Enhanced production of validamycin A by H2O2-induced reactive oxygen species in fermentation of Streptomyces hygroscopicus 5008
    • Wei ZH, Bai L, Deng Z, Zhong JJ. 2011. Enhanced production of validamycin A by H2O2-induced reactive oxygen species in fermentation of Streptomyces hygroscopicus 5008. Bioresour. Technol. 102:1783-1787.
    • (2011) Bioresour. Technol. , vol.102 , pp. 1783-1787
    • Wei, Z.H.1    Bai, L.2    Deng, Z.3    Zhong, J.J.4
  • 65
    • 84866334129 scopus 로고    scopus 로고
    • The second messenger cyclic di-GMP
    • ed, Washington, DC
    • Wolf A, Visick K (ed). 2010. The second messenger cyclic di-GMP, p 356. ASM Press, Washington, DC.
    • (2010) ASM Press , pp. 356
    • Wolf, A.1    Visick, K.2


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