메뉴 건너뛰기




Volumn 428, Issue 19, 2016, Pages 3683-3701

C-di-GMP Synthesis: Structural Aspects of Evolution, Catalysis and Regulation

Author keywords

diguanylate cyclase; regulation; second messenger; signal transduction; signaling

Indexed keywords

ADENYLATE CYCLASE; CYCLIC DI GUANOSINE MONOPHOSPHATE; DIGUANYLATE CYCLASE; DIMER; GLOBIN; GLOBIN COUPLED SENSOR; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATE; MONOMER; PELD RECEPTOR; PHOSPHODIESTERASE; PROTEIN HISTIDINE KINASE; RECEPTOR; UNCLASSIFIED DRUG; BIS(3',5')-CYCLIC DIGUANYLIC ACID; CYCLIC GMP; ESCHERICHIA COLI PROTEIN; LYASE;

EID: 84986922030     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2016.07.023     Document Type: Review
Times cited : (112)

References (77)
  • 1
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: mechanisms of signalling
    • [1] Mills, E., Pultz, I.S., Kulasekara, H.D., Miller, S.I., The bacterial second messenger c-di-GMP: mechanisms of signalling. Cell. Microbiol. 13 (2011), 1122–1129, 10.1111/j.1462-5822.2011.01619.x.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1122-1129
    • Mills, E.1    Pultz, I.S.2    Kulasekara, H.D.3    Miller, S.I.4
  • 2
    • 84870208079 scopus 로고    scopus 로고
    • Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems
    • [2] Boyd, C.D., O'Toole, G.A., Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems. Annu. Rev. Cell Dev. Biol. 28 (2012), 439–462, 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
  • 3
    • 84953923744 scopus 로고    scopus 로고
    • Bacterial signal transduction by c-di-GMP and other nucleotide second messengers
    • [3] Hengge, R., Gründling, A., Jenal, U., Ryan, R., Yildiz, F., Bacterial signal transduction by c-di-GMP and other nucleotide second messengers. J. Bacteriol. 198 (2015), 15–26, 10.1128/JB.00331-15.
    • (2015) J. Bacteriol. , vol.198 , pp. 15-26
    • Hengge, R.1    Gründling, A.2    Jenal, U.3    Ryan, R.4    Yildiz, F.5
  • 4
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • [4] Tamayo, R., Pratt, J.T., Camilli, A., Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu. Rev. Microbiol. 61 (2007), 131–148, 10.1146/annurev.micro.61.080706.093426.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 5
    • 84864052471 scopus 로고    scopus 로고
    • The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways
    • [5] Malone, J.G., Jaeger, T., Manfredi, P., Dötsch, A., Blanka, A., Bos, R., et al. The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways. PLoS Pathog. 8 (2012), 1–19, e1002760, 10.1371/journal.ppat.1002760.
    • (2012) PLoS Pathog. , vol.8 , pp. 1-19
    • Malone, J.G.1    Jaeger, T.2    Manfredi, P.3    Dötsch, A.4    Blanka, A.5    Bos, R.6
  • 6
    • 84924674555 scopus 로고    scopus 로고
    • Identification and characterization of VpsR and VpsT binding sites in Vibrio cholerae
    • [6] Zamorano-Sánchez, D., Fong, J.C.N., Kilic, S., Erill, I., Yildiz, F.H., Identification and characterization of VpsR and VpsT binding sites in Vibrio cholerae. J. Bacteriol. 197 (2015), 1221–1235, 10.1128/JB.02439-14.
    • (2015) J. Bacteriol. , vol.197 , pp. 1221-1235
    • Zamorano-Sánchez, D.1    Fong, J.C.N.2    Kilic, S.3    Erill, I.4    Yildiz, F.H.5
  • 7
    • 84974577707 scopus 로고    scopus 로고
    • A. Filloux, biofilms and cyclic di-GMP (c-di-GMP) signaling: lessons from Pseudomonas aeruginosa and other bacteria
    • [7] Valentini, M., A. Filloux, biofilms and cyclic di-GMP (c-di-GMP) signaling: lessons from Pseudomonas aeruginosa and other bacteria. J. Biol. Chem. 291 (2016), 12,547–12,555, 10.1074/jbc.R115.711507.
    • (2016) J. Biol. Chem. , vol.291 , pp. 12547-12555
    • Valentini, M.1
  • 9
    • 84966273607 scopus 로고    scopus 로고
    • Comparative genomic analyses reveal a vast, novel network of nucleotide-centric systems in biological conflicts, immunity and signaling
    • [9] Burroughs, A.M., Zhang, D., Schäffer, D.E., Iyer, L.M., Aravind, L., Comparative genomic analyses reveal a vast, novel network of nucleotide-centric systems in biological conflicts, immunity and signaling. Nucleic Acids Res. 43 (2015), 10,633–10,654, 10.1093/nar/gkv1267.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 10633-10654
    • Burroughs, A.M.1    Zhang, D.2    Schäffer, D.E.3    Iyer, L.M.4    Aravind, L.5
  • 10
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: the first 25 years of a universal bacterial second messenger
    • [10] Römling, U., Galperin, M.Y., Gomelsky, M., Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol. Mol. Biol. Rev. 77 (2013), 1–52, 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
  • 11
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • [11] Schirmer, T., Jenal, U., Structural and mechanistic determinants of c-di-GMP signalling. Nat. Rev. Microbiol. 7 (2009), 724–735, 10.1038/nrmicro2203.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 12
    • 84862527194 scopus 로고    scopus 로고
    • Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP
    • [12] Krasteva, P.V., Giglio, K.M., Sondermann, H., Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP. Protein Sci. 21 (2012), 929–948, 10.1002/pro.2093.
    • (2012) Protein Sci. , vol.21 , pp. 929-948
    • Krasteva, P.V.1    Giglio, K.M.2    Sondermann, H.3
  • 13
    • 84953924413 scopus 로고    scopus 로고
    • Diversity of cyclic di-GMP-binding proteins and mechanisms
    • [13] Chou, S.-H., Galperin, M.Y., Diversity of cyclic di-GMP-binding proteins and mechanisms. J. Bacteriol. 198 (2016), 32–46, 10.1128/JB.00333-15.
    • (2016) J. Bacteriol. , vol.198 , pp. 32-46
    • Chou, S.-H.1    Galperin, M.Y.2
  • 14
    • 84922947346 scopus 로고    scopus 로고
    • Bacterial diguanylate cyclases: structure, function and mechanism in exopolysaccharide biofilm development
    • [14] Whiteley, C.G., Lee, D.-J., Bacterial diguanylate cyclases: structure, function and mechanism in exopolysaccharide biofilm development. Biotechnol. Adv. 33 (2015), 124–141, 10.1016/j.biotechadv.2014.11.010.
    • (2015) Biotechnol. Adv. , vol.33 , pp. 124-141
    • Whiteley, C.G.1    Lee, D.-J.2
  • 15
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • [15] Möglich, A., Ayers, R.A., Moffat, K., Structure and signaling mechanism of Per-ARNT-Sim domains. Structure 17 (2009), 1282–1294, 10.1016/j.str.2009.08.011.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 16
    • 84879836986 scopus 로고    scopus 로고
    • Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators
    • [16] Diensthuber, R.P., Bommer, M., Gleichmann, T., Möglich, A., Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators. Structure 21 (2013), 1127–1136, 10.1016/j.str.2013.04.024.
    • (2013) Structure , vol.21 , pp. 1127-1136
    • Diensthuber, R.P.1    Bommer, M.2    Gleichmann, T.3    Möglich, A.4
  • 17
    • 84930376521 scopus 로고    scopus 로고
    • Signal transduction in histidine kinases: insights from new structures
    • [17] Bhate, M.P., Molnar, K.S., Goulian, M., DeGrado, W.F., Signal transduction in histidine kinases: insights from new structures. Structure 23 (2015), 981–994, 10.1016/j.str.2015.04.002.
    • (2015) Structure , vol.23 , pp. 981-994
    • Bhate, M.P.1    Molnar, K.S.2    Goulian, M.3    DeGrado, W.F.4
  • 19
    • 0027370179 scopus 로고
    • Molecular structure of cyclic diguanylic acid at 1 A resolution of two crystal forms: self-association, interactions with metal ion/planar dyes and modeling studies
    • [19] Guan, Y., Gao, Y., Liaw, Y., Robinson, H., Wang, A., Molecular structure of cyclic diguanylic acid at 1 A resolution of two crystal forms: self-association, interactions with metal ion/planar dyes and modeling studies. J. Biomol. Struct. Dyn. 11 (1993), 253–276.
    • (1993) J. Biomol. Struct. Dyn. , vol.11 , pp. 253-276
    • Guan, Y.1    Gao, Y.2    Liaw, Y.3    Robinson, H.4    Wang, A.5
  • 20
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • [20] Chan, C., Paul, R., Samoray, D., Amiot, N.C., Giese, B., Jenal, U., et al. Structural basis of activity and allosteric control of diguanylate cyclase. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 17,084–17,089, 10.1073/pnas.0406134101.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17084-17089
    • Chan, C.1    Paul, R.2    Samoray, D.3    Amiot, N.C.4    Giese, B.5    Jenal, U.6
  • 21
    • 77950859347 scopus 로고    scopus 로고
    • Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins
    • [21] Ko, J., Ryu, K.-S., Kim, H., Shin, J.-S., Lee, J.-O., Cheong, C., et al. Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins. J. Mol. Biol. 398 (2010), 97–110, 10.1016/j.jmb.2010.03.007.
    • (2010) J. Mol. Biol. , vol.398 , pp. 97-110
    • Ko, J.1    Ryu, K.-S.2    Kim, H.3    Shin, J.-S.4    Lee, J.-O.5    Cheong, C.6
  • 22
    • 33744904451 scopus 로고    scopus 로고
    • Polymorphism of the signaling molecule c-di-GMP
    • [22] Zhang, Z., Kim, S., Gaffney, B.L., Jones, R.A., Polymorphism of the signaling molecule c-di-GMP. J. Am. Chem. Soc. 128 (2006), 7015–7024, 10.1021/ja0613714.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7015-7024
    • Zhang, Z.1    Kim, S.2    Gaffney, B.L.3    Jones, R.A.4
  • 23
    • 84855952253 scopus 로고    scopus 로고
    • Oligomer formation of the bacterial second messenger c-di-GMP: reaction rates and equilibrium constants indicate a monomeric state at physiological concentrations
    • [23] Gentner, M., Allan, M.G., Zaehringer, F., Schirmer, T., Grzesiek, S., Oligomer formation of the bacterial second messenger c-di-GMP: reaction rates and equilibrium constants indicate a monomeric state at physiological concentrations. J. Am. Chem. Soc. 134 (2012), 1019–1029, 10.1021/ja207742q.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1019-1029
    • Gentner, M.1    Allan, M.G.2    Zaehringer, F.3    Schirmer, T.4    Grzesiek, S.5
  • 24
    • 0035254950 scopus 로고    scopus 로고
    • GGDEF domain is homologous to adenylyl cyclase
    • [24] Pei, J., Grishin, N.V., GGDEF domain is homologous to adenylyl cyclase. Proteins. 42 (2001), 210–216.
    • (2001) Proteins. , vol.42 , pp. 210-216
    • Pei, J.1    Grishin, N.V.2
  • 25
    • 84919337973 scopus 로고    scopus 로고
    • Structure, mechanism, and regulation of soluble adenylyl cyclases - similarities and differences to transmembrane adenylyl cyclases
    • [25] Steegborn, C., Structure, mechanism, and regulation of soluble adenylyl cyclases - similarities and differences to transmembrane adenylyl cyclases. Biochim. Biophys. Acta. 1842 (2014), 2535–2547, 10.1016/j.bbadis.2014.08.012.
    • (2014) Biochim. Biophys. Acta. , vol.1842 , pp. 2535-2547
    • Steegborn, C.1
  • 26
    • 33751438617 scopus 로고    scopus 로고
    • Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases
    • [26] Sinha, S.C., Sprang, S.R., Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases. Rev. Physiol. Biochem. Pharmacol. 157 (2006), 105–140.
    • (2006) Rev. Physiol. Biochem. Pharmacol. , vol.157 , pp. 105-140
    • Sinha, S.C.1    Sprang, S.R.2
  • 27
    • 84959440981 scopus 로고    scopus 로고
    • Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3″, 3-″cGAMP)
    • [27] Hallberg, Z.F., Wang, X.C., Wright, T.A., Nan, B., Ad, O., Yeo, J., et al. Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3″, 3-″cGAMP). Proc. Natl. Acad. Sci. U. S. A. 113 (2016), 1790–1795, 10.1073/pnas.1515287113.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. 1790-1795
    • Hallberg, Z.F.1    Wang, X.C.2    Wright, T.A.3    Nan, B.4    Ad, O.5    Yeo, J.6
  • 28
    • 84879826686 scopus 로고    scopus 로고
    • Structure and signaling mechanism of a zinc-sensory diguanylate cyclase
    • [28] Zähringer, F., Lacanna, E., Jenal, U., Schirmer, T., Boehm, A., Structure and signaling mechanism of a zinc-sensory diguanylate cyclase. Structure 21 (2013), 1149–1157, 10.1016/j.str.2013.04.026.
    • (2013) Structure , vol.21 , pp. 1149-1157
    • Zähringer, F.1    Lacanna, E.2    Jenal, U.3    Schirmer, T.4    Boehm, A.5
  • 29
    • 82455163827 scopus 로고    scopus 로고
    • The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)(2) at the active site
    • [29] Yang, C.-Y., Chin, K.-H., Chuah, M.L.C., Liang, Z.-X., Wang, A.H.-J., Chou, S.-H., The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)(2) at the active site. Acta Crystallogr. D Biol. Crystallogr. 67 (2011), 997–1008, 10.1107/S090744491104039X.
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 997-1008
    • Yang, C.-Y.1    Chin, K.-H.2    Chuah, M.L.C.3    Liang, Z.-X.4    Wang, A.H.-J.5    Chou, S.-H.6
  • 31
    • 11444256177 scopus 로고    scopus 로고
    • Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment
    • [31] Steegborn, C., Litvin, T.N., Levin, L.R., Buck, J., Wu, H., Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment. Nat. Struct. Mol. Biol. 12 (2005), 32–37, 10.1038/nsmb880.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 32-37
    • Steegborn, C.1    Litvin, T.N.2    Levin, L.R.3    Buck, J.4    Wu, H.5
  • 33
    • 84909992740 scopus 로고    scopus 로고
    • Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability
    • [33] Deepthi, A., Liew, C.W., Liang, Z.-X., Swaminathan, K., Lescar, J., Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability. PLoS One 9 (2014), 1–9, e110912, 10.1371/journal.pone.0110912.
    • (2014) PLoS One , vol.9 , pp. 1-9
    • Deepthi, A.1    Liew, C.W.2    Liang, Z.-X.3    Swaminathan, K.4    Lescar, J.5
  • 34
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • [34] Wassmann, P., Chan, C., Paul, R., Beck, A., Heerklotz, H., Jenal, U., et al. Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15 (2007), 915–927, 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
  • 35
    • 67349108043 scopus 로고    scopus 로고
    • Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
    • [35] Rao, F., Pasunooti, S., Ng, Y., Zhuo, W., Lim, L., Liu, A.W., et al. Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase. Anal. Biochem. 389 (2009), 138–142, 10.1016/j.ab.2009.03.031.
    • (2009) Anal. Biochem. , vol.389 , pp. 138-142
    • Rao, F.1    Pasunooti, S.2    Ng, Y.3    Zhuo, W.4    Lim, L.5    Liu, A.W.6
  • 36
    • 63449138218 scopus 로고    scopus 로고
    • The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic di-GMP in host cell infection
    • [36] Lai, T.-H., Kumagai, Y., Hyodo, M., Hayakawa, Y., Rikihisa, Y., The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic di-GMP in host cell infection. J. Bacteriol. 191 (2009), 693–700, 10.1128/JB.01218-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 693-700
    • Lai, T.-H.1    Kumagai, Y.2    Hyodo, M.3    Hayakawa, Y.4    Rikihisa, Y.5
  • 37
    • 70349783823 scopus 로고    scopus 로고
    • Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
    • [37] De, N., Navarro, M.V.A.S., Raghavan, R.V., Sondermann, H., Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR. J. Mol. Biol. 393 (2009), 619–633, 10.1016/j.jmb.2009.08.030.
    • (2009) J. Mol. Biol. , vol.393 , pp. 619-633
    • De, N.1    Navarro, M.V.A.S.2    Raghavan, R.V.3    Sondermann, H.4
  • 38
    • 84896718101 scopus 로고    scopus 로고
    • Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: clues from the structure of the catalytic domain
    • [38] Giardina, G., Paiardini, A., Fernicola, S., Franceschini, S., Rinaldo, S., Stelitano, V., et al. Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: clues from the structure of the catalytic domain. PLoS One 8 (2013), 1–15, e81324, 10.1371/journal.pone.0081324.
    • (2013) PLoS One , vol.8 , pp. 1-15
    • Giardina, G.1    Paiardini, A.2    Fernicola, S.3    Franceschini, S.4    Rinaldo, S.5    Stelitano, V.6
  • 39
    • 48549093368 scopus 로고    scopus 로고
    • MSDmotif: exploring protein sites and motifs
    • [39] Golovin, A., Henrick, K., MSDmotif: exploring protein sites and motifs. BMC Bioinformatics, 9, 2008, 312, 10.1186/1471-2105-9-312.
    • (2008) BMC Bioinformatics , vol.9 , pp. 312
    • Golovin, A.1    Henrick, K.2
  • 40
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
    • [40] Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H., Jenal, U., Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J. Biol. Chem. 282 (2007), 29,170–29,177, 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
  • 41
    • 84861801044 scopus 로고    scopus 로고
    • You've come a long way: c-di-GMP signaling
    • [41] Sondermann, H., Shikuma, N.J., Yildiz, F.H., You've come a long way: c-di-GMP signaling. Curr. Opin. Microbiol. 15 (2012), 140–146, 10.1016/j.mib.2011.12.008.
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 140-146
    • Sondermann, H.1    Shikuma, N.J.2    Yildiz, F.H.3
  • 42
    • 84879571298 scopus 로고    scopus 로고
    • Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity
    • [42] Huangyutitham, V., Güvener, Z.T., Harwood, C.S., Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity. MBio 4 (2013), 1–8, e00242–13, 10.1128/mBio.00242-13.
    • (2013) MBio , vol.4 , pp. 1-8
    • Huangyutitham, V.1    Güvener, Z.T.2    Harwood, C.S.3
  • 43
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
    • [43] Ryjenkov, D.A., Tarutina, M., Moskvin, O.V., Gomelsky, M., Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187 (2005), 1792–1798, 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
  • 44
    • 84884781778 scopus 로고    scopus 로고
    • Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis
    • [44] Martínková, M., Kitanishi, K., Shimizu, T., Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis. J. Biol. Chem. 288 (2013), 27,702–27,711, 10.1074/jbc.R113.473249.
    • (2013) J. Biol. Chem. , vol.288 , pp. 27702-27711
    • Martínková, M.1    Kitanishi, K.2    Shimizu, T.3
  • 45
    • 84907646721 scopus 로고    scopus 로고
    • Oligomeric state affects oxygen dissociation and diguanylate cyclase activity of globin coupled sensors
    • [45] Burns, J.L., Deer, D.D., Weinert, E.E., Oligomeric state affects oxygen dissociation and diguanylate cyclase activity of globin coupled sensors. Mol. BioSyst. 10 (2014), 2823–2826, 10.1039/c4mb00366g.
    • (2014) Mol. BioSyst. , vol.10 , pp. 2823-2826
    • Burns, J.L.1    Deer, D.D.2    Weinert, E.E.3
  • 46
    • 70350047301 scopus 로고    scopus 로고
    • An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
    • [46] Tuckerman, J.R., Gonzalez, G., Sousa, E.H.S., Wan, X., Saito, J.A., Alam, M., et al. An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 48 (2009), 9764–9774, 10.1021/bi901409g.
    • (2009) Biochemistry , vol.48 , pp. 9764-9774
    • Tuckerman, J.R.1    Gonzalez, G.2    Sousa, E.H.S.3    Wan, X.4    Saito, J.A.5    Alam, M.6
  • 47
    • 71649089775 scopus 로고    scopus 로고
    • Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP
    • [47] Sawai, H., Yoshioka, S., Uchida, T., Hyodo, M., Hayakawa, Y., Ishimori, K., et al. Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP. Biochim. Biophys. Acta 1804 (2010), 166–172, 10.1016/j.bbapap.2009.09.028.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 166-172
    • Sawai, H.1    Yoshioka, S.2    Uchida, T.3    Hyodo, M.4    Hayakawa, Y.5    Ishimori, K.6
  • 48
    • 84868144315 scopus 로고    scopus 로고
    • A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase
    • [48] Schaller, R.A., Ali, S.K., Klose, K.E., Kurtz, D.M., A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase. Biochemistry. 51 (2012), 8563–8570, 10.1021/bi3011797.
    • (2012) Biochemistry. , vol.51 , pp. 8563-8570
    • Schaller, R.A.1    Ali, S.K.2    Klose, K.E.3    Kurtz, D.M.4
  • 49
    • 70350501347 scopus 로고    scopus 로고
    • A Flavin Cofactor-Binding PAS Domain Regulates c-di-GMP Synthesis in AxDGC2 from Acetobacter xylinum
    • [49] Qi, Y., Rao, F., Luo, Z., Liang, Z.X., A Flavin Cofactor-Binding PAS Domain Regulates c-di-GMP Synthesis in AxDGC2 from Acetobacter xylinum. Biochemistry. 48 (2009), 10275–10285.
    • (2009) Biochemistry. , vol.48 , pp. 10275-10285
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.X.4
  • 50
    • 33947412138 scopus 로고    scopus 로고
    • Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: signaling, dimerization, and mechanism
    • [50] Key, J., Hefti, M., Purcell, E.B., Moffat, K., Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: signaling, dimerization, and mechanism. Biochemistry. 46 (2007), 3614–3623, 10.1021/bi0620407.
    • (2007) Biochemistry. , vol.46 , pp. 3614-3623
    • Key, J.1    Hefti, M.2    Purcell, E.B.3    Moffat, K.4
  • 51
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • [51] Söding, J., Protein homology detection by HMM-HMM comparison. Bioinformatics. 21 (2005), 951–960, 10.1093/bioinformatics/bti125.
    • (2005) Bioinformatics. , vol.21 , pp. 951-960
    • Söding, J.1
  • 52
    • 70849084890 scopus 로고    scopus 로고
    • Mechanism for the allosteric regulation of phosphodiesterase 2 A deduced from the X-ray structure of a near full-length construct
    • [52] Pandit, J., Forman, M.D., Fennell, K.F., Dillman, K.S., Menniti, F.S., Mechanism for the allosteric regulation of phosphodiesterase 2 A deduced from the X-ray structure of a near full-length construct. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 18,225–18,230, 10.1073/pnas.0907635106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 18225-18230
    • Pandit, J.1    Forman, M.D.2    Fennell, K.F.3    Dillman, K.S.4    Menniti, F.S.5
  • 53
    • 0036790852 scopus 로고    scopus 로고
    • The two GAF domains in phosphodiesterase 2 A have distinct roles in dimerization and in cGMP binding
    • [53] Martinez, S.E., Wu, A.Y., Glavas, N.A., Tang, X.-B., Turley, S., Hol, W.G.J., et al. The two GAF domains in phosphodiesterase 2 A have distinct roles in dimerization and in cGMP binding. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 13,260–13,265, 10.1073/pnas.192374899.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13260-13265
    • Martinez, S.E.1    Wu, A.Y.2    Glavas, N.A.3    Tang, X.-B.4    Turley, S.5    Hol, W.G.J.6
  • 54
    • 71249129667 scopus 로고    scopus 로고
    • Cyclic nucleotide binding GAF domains from phosphodiesterases: structural and mechanistic insights
    • [54] Heikaus, C.C., Pandit, J., Klevit, R.E., Cyclic nucleotide binding GAF domains from phosphodiesterases: structural and mechanistic insights. Structure. 17 (2009), 1551–1557, 10.1016/j.str.2009.07.019.
    • (2009) Structure. , vol.17 , pp. 1551-1557
    • Heikaus, C.C.1    Pandit, J.2    Klevit, R.E.3
  • 55
    • 84884292053 scopus 로고    scopus 로고
    • A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis
    • [55] An, S.-Q., Chin, K.-H., Febrer, M., McCarthy, Y., Yang, J.-G., Liu, C.-L., et al. A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis. EMBO J. 32 (2013), 2430–2438, 10.1038/emboj.2013.165.
    • (2013) EMBO J. , vol.32 , pp. 2430-2438
    • An, S.-Q.1    Chin, K.-H.2    Febrer, M.3    McCarthy, Y.4    Yang, J.-G.5    Liu, C.-L.6
  • 56
    • 66349083528 scopus 로고    scopus 로고
    • Structural basis for cAMP-mediated allosteric control of the catabolite activator protein
    • [56] Popovych, N., Tzeng, S.R., Tonelli, M., Ebright, R.H., Kalodimos, C.G., Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 6927–6932, 10.1073/pnas.0900595106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 6927-6932
    • Popovych, N.1    Tzeng, S.R.2    Tonelli, M.3    Ebright, R.H.4    Kalodimos, C.G.5
  • 57
    • 70349734666 scopus 로고    scopus 로고
    • Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
    • [57] Sharma, H., Yu, S., Kong, J., Wang, J., Steitz, T.A., Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 16,604–16,609, 10.1073/pnas.0908380106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16604-16609
    • Sharma, H.1    Yu, S.2    Kong, J.3    Wang, J.4    Steitz, T.A.5
  • 58
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP
    • [58] Tarutina, M., Ryjenkov, D.A., Gomelsky, M., An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP. J. Biol. Chem. 281 (2006), 34,751–34,758, 10.1074/jbc.M604819200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 59
    • 84904314045 scopus 로고    scopus 로고
    • Near-infrared light responsive synthetic c-di-GMP module for optogenetic applications
    • [59] Ryu, M.-H., Gomelsky, M., Near-infrared light responsive synthetic c-di-GMP module for optogenetic applications. ACS Synth. Biol. 3 (2014), 802–810, 10.1021/sb400182x.
    • (2014) ACS Synth. Biol. , vol.3 , pp. 802-810
    • Ryu, M.-H.1    Gomelsky, M.2
  • 60
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction
    • [60] Yang, X., Kuk, J., Moffat, K., Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 14,715–14,720, 10.1073/pnas.0806718105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 61
    • 84964854422 scopus 로고    scopus 로고
    • Structure of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris provides clues to its long-range signaling mechanism
    • [61] Otero, L.H., Klinke, S., Rinaldi, J., Velázquez-Escobar, F., Mroginski, M.A., Fernández López, M., et al. Structure of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris provides clues to its long-range signaling mechanism. J. Mol. Biol. 428 (2016), 3702–3720.
    • (2016) J. Mol. Biol. , vol.428 , pp. 3702-3720
    • Otero, L.H.1    Klinke, S.2    Rinaldi, J.3    Velázquez-Escobar, F.4    Mroginski, M.A.5    Fernández López, M.6
  • 62
    • 84865741837 scopus 로고    scopus 로고
    • Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1
    • [62] Li, Z., Chen, J.-H., Hao, Y., Nair, S.K., Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 287 (2012), 30,191–30,204, 10.1074/jbc.M112.378273.
    • (2012) J. Biol. Chem. , vol.287 , pp. 30191-30204
    • Li, Z.1    Chen, J.-H.2    Hao, Y.3    Nair, S.K.4
  • 63
    • 84863611012 scopus 로고    scopus 로고
    • Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa
    • [63] Whitney, J.C., Colvin, K.M., Marmont, L.S., Robinson, H., Parsek, M.R., Howell, P.L., Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa. J. Biol. Chem. 287 (2012), 23,582–23,593, 10.1074/jbc.M112.375378.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23582-23593
    • Whitney, J.C.1    Colvin, K.M.2    Marmont, L.S.3    Robinson, H.4    Parsek, M.R.5    Howell, P.L.6
  • 64
    • 84907835236 scopus 로고    scopus 로고
    • The disulfide bonding system suppresses CsgD-independent cellulose production in Escherichia coli
    • [64] Hufnagel, D.A., DePas, W.H., Chapman, M.R., The disulfide bonding system suppresses CsgD-independent cellulose production in Escherichia coli. J. Bacteriol. 196 (2014), 3690–3699, 10.1128/jb.02019-14.
    • (2014) J. Bacteriol. , vol.196 , pp. 3690-3699
    • Hufnagel, D.A.1    DePas, W.H.2    Chapman, M.R.3
  • 65
    • 75149162101 scopus 로고    scopus 로고
    • The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12
    • [65] Stewart, V., Chen, L.-L., The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12. J. Bacteriol. 192 (2010), 734–745, 10.1128/JB.00172-09.
    • (2010) J. Bacteriol. , vol.192 , pp. 734-745
    • Stewart, V.1    Chen, L.-L.2
  • 66
    • 84929417365 scopus 로고    scopus 로고
    • Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ
    • [66] Molnar, K.S., Bonomi, M., Pellarin, R., Clinthorne, G.D., Gonzalez, G., Goldberg, S.D., et al. Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ. Structure 22 (2014), 1239–1251, 10.1016/j.str.2014.04.019.
    • (2014) Structure , vol.22 , pp. 1239-1251
    • Molnar, K.S.1    Bonomi, M.2    Pellarin, R.3    Clinthorne, G.D.4    Gonzalez, G.5    Goldberg, S.D.6
  • 67
    • 77950405367 scopus 로고    scopus 로고
    • YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa
    • [67] Malone, J.G., Jaeger, T., Spangler, C., Ritz, D., Spang, A., Arrieumerlou, C., et al. YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa. PLoS Pathog. 6 (2010), 1–17, e1000804, 10.1371/journal.ppat.1000804.
    • (2010) PLoS Pathog. , vol.6 , pp. 1-17
    • Malone, J.G.1    Jaeger, T.2    Spangler, C.3    Ritz, D.4    Spang, A.5    Arrieumerlou, C.6
  • 68
    • 84929998937 scopus 로고    scopus 로고
    • Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP
    • [68] Chatterjee, D., Cooley, R.B., Boyd, C.D., Mehl, R.A., O'Toole, G.A., Sondermann, H., Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP. Elife 3 (2014), 1–29, e03650.
    • (2014) Elife , vol.3 , pp. 1-29
    • Chatterjee, D.1    Cooley, R.B.2    Boyd, C.D.3    Mehl, R.A.4    O'Toole, G.A.5    Sondermann, H.6
  • 69
    • 84901621471 scopus 로고    scopus 로고
    • A soluble mutant of the transmembrane receptor Af1503 features strong changes in coiled-coil periodicity
    • [69] Hartmann, M.D., Dunin-Horkawicz, S., Hulko, M., Martin, J., Coles, M., Lupas, A.N., A soluble mutant of the transmembrane receptor Af1503 features strong changes in coiled-coil periodicity. J. Struct. Biol. 186 (2014), 357–366, 10.1016/j.jsb.2014.02.008.
    • (2014) J. Struct. Biol. , vol.186 , pp. 357-366
    • Hartmann, M.D.1    Dunin-Horkawicz, S.2    Hulko, M.3    Martin, J.4    Coles, M.5    Lupas, A.N.6
  • 70
    • 79952260048 scopus 로고    scopus 로고
    • Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis
    • [70] Navarro, M.V.A.S., Newell, P.D., Krasteva, P.V., Chatterjee, D., Madden, D.R., O'Toole, G.A., et al. Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis. PLoS Biol. 9 (2011), 1–21, e1000588, 10.1371/journal.pbio.1000588.
    • (2011) PLoS Biol. , vol.9 , pp. 1-21
    • Navarro, M.V.A.S.1    Newell, P.D.2    Krasteva, P.V.3    Chatterjee, D.4    Madden, D.R.5    O'Toole, G.A.6
  • 72
    • 64449088389 scopus 로고    scopus 로고
    • Globins synthesize the second messenger bis-(3″-5″)-cyclic diguanosine monophosphate in bacteria
    • [72] Wan, X., Tuckerman, J.R., Saito, J.A., Freitas, T.A.K., Newhouse, J.S., Denery, J.R., et al. Globins synthesize the second messenger bis-(3″-5″)-cyclic diguanosine monophosphate in bacteria. J. Mol. Biol. 388 (2009), 262–270, 10.1016/j.jmb.2009.03.015.
    • (2009) J. Mol. Biol. , vol.388 , pp. 262-270
    • Wan, X.1    Tuckerman, J.R.2    Saito, J.A.3    Freitas, T.A.K.4    Newhouse, J.S.5    Denery, J.R.6
  • 73
    • 0036308878 scopus 로고    scopus 로고
    • Cation-pi/H-bond stair motifs at protein-DNA interfaces
    • [73] Rooman, M., Liévin, J., Buisine, E., Wintjens, R., Cation-pi/H-bond stair motifs at protein-DNA interfaces. J. Mol. Biol. 319 (2002), 67–76.
    • (2002) J. Mol. Biol. , vol.319 , pp. 67-76
    • Rooman, M.1    Liévin, J.2    Buisine, E.3    Wintjens, R.4
  • 74
    • 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
    • [74] Bharati, B.K., Sharma, I.M., Kasetty, S., Kumar, M., Mukherjee, R., Chatterji, D., 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 (2012), 1415–1427, 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
  • 75
    • 84915756720 scopus 로고    scopus 로고
    • Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator
    • [75] Phippen, C.W., Mikolajek, H., Schlaefli, H.G., Keevil, C.W., Webb, J.S., Tews, I., Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator. FEBS Lett. 588 (2014), 4631–4636, 10.1016/j.febslet.2014.11.002.
    • (2014) FEBS Lett. , vol.588 , pp. 4631-4636
    • Phippen, C.W.1    Mikolajek, H.2    Schlaefli, H.G.3    Keevil, C.W.4    Webb, J.S.5    Tews, I.6
  • 76
    • 84896790464 scopus 로고    scopus 로고
    • Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger cyclic di-GMP
    • [76] Sundriyal, A., Massa, C., Samoray, D., Zehender, F., Sharpe, T., Jenal, U., et al. Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger cyclic di-GMP. J. Biol. Chem. 289 (2014), 6978–6990, 10.1074/jbc.M113.516195.
    • (2014) J. Biol. Chem. , vol.289 , pp. 6978-6990
    • Sundriyal, A.1    Massa, C.2    Samoray, D.3    Zehender, F.4    Sharpe, T.5    Jenal, U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.