메뉴 건너뛰기




Volumn 53, Issue 13, 2014, Pages 2126-2135

A structural basis for the regulation of an H-NOX-associated cyclic-di-GMP synthase/phosphodiesterase enzyme by nitric oxide-bound H-NOX

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ENZYMES; GENE ENCODING; MOLECULES; NITRIC OXIDE; PROTEINS;

EID: 84898043101     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401597m     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 2642554922 scopus 로고    scopus 로고
    • Bacterial signal transduction network in a genomic perspective
    • Galperin, M. Y. (2004) Bacterial signal transduction network in a genomic perspective Environ. Microbiol. 6 (6) 552-567
    • (2004) Environ. Microbiol. , vol.6 , Issue.6 , pp. 552-567
    • Galperin, M.Y.1
  • 2
    • 66749083981 scopus 로고    scopus 로고
    • Signals, regulatory networks, and materials that build and break bacterial biofilms
    • Karatan, E. and Watnick, P. (2009) Signals, regulatory networks, and materials that build and break bacterial biofilms Microbiol. Mol. Biol. Rev. 73 (2) 310-347
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , Issue.2 , pp. 310-347
    • Karatan, E.1    Watnick, P.2
  • 3
    • 4444250897 scopus 로고    scopus 로고
    • Cyclic-di-GMP as a bacterial second messenger
    • D'Argenio, D. A. and Miller, S. I. (2004) Cyclic-di-GMP as a bacterial second messenger Microbiology 150 (Part 8) 2497-2502
    • (2004) Microbiology , vol.150 , Issue.PART 8 , pp. 2497-2502
    • D'Argenio, D.A.1    Miller, S.I.2
  • 4
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria
    • Jenal, U. (2004) Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria Curr. Opin. Microbiol. 7 (2) 185-191
    • (2004) Curr. Opin. Microbiol. , vol.7 , Issue.2 , pp. 185-191
    • Jenal, U.1
  • 5
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal, U. and Malone, J. (2006) Mechanisms of cyclic-di-GMP signaling in bacteria Annu. Rev. Genet. 40, 385-407
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 6
    • 33846847846 scopus 로고    scopus 로고
    • C-di-GMP-mediated regulation of virulence and biofilm formation
    • Cotter, P. A. and Stibitz, S. (2007) C-di-GMP-mediated regulation of virulence and biofilm formation Curr. Opin. Microbiol. 10 (1) 17-23
    • (2007) Curr. Opin. Microbiol. , vol.10 , Issue.1 , pp. 17-23
    • Cotter, P.A.1    Stibitz, S.2
  • 7
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo, R., Pratt, J. T., and 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
  • 8
    • 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 (4) 263-273
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.4 , pp. 263-273
    • Hengge, R.1
  • 9
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge, P., Paul, R., Patrick, G., Rainey, P., and Jenal, U. (2003) Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus Mol. Microbiol. 47 (6) 1695-1708
    • (2003) Mol. Microbiol. , vol.47 , Issue.6 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Patrick, G.3    Rainey, P.4    Jenal, U.5
  • 10
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer, L., Anantharaman, V., and Aravind, L. (2003) Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins BMC Genomics 4 (1) 1-8
    • (2003) BMC Genomics , vol.4 , Issue.1 , pp. 1-8
    • Iyer, L.1    Anantharaman, V.2    Aravind, L.3
  • 11
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov, D. A., Tarutina, M., Moskvin, O. V., and Gomelsky, M. (2005) Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain J. Bacteriol. 187 (5) 1792-1808
    • (2005) J. Bacteriol. , vol.187 , Issue.5 , pp. 1792-1808
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 12
    • 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., and Jenal, U. (2005) Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP J. Biol. Chem. 280 (35) 30829-30837
    • (2005) J. Biol. Chem. , vol.280 , Issue.35 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 13
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
    • Schmidt, A. J., Ryjenkov, D. A., and Gomelsky, M. (2005) The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains J. Bacteriol. 187 (14) 4774-4781
    • (2005) J. Bacteriol. , vol.187 , Issue.14 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 15
    • 0032902722 scopus 로고    scopus 로고
    • Guanylate cyclase and the NO/cGMP signaling pathway
    • Denninger, J. W. and Marletta, M. A. (1999) Guanylate cyclase and the NO/cGMP signaling pathway Biochim. Biophys. Acta 1411, 334-350
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 334-350
    • Denninger, J.W.1    Marletta, M.A.2
  • 16
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005) A molecular basis for NO selectivity in soluble guanylate cyclase Nat. Chem. Biol. 1 (1) 53-59
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 17
    • 72249092095 scopus 로고    scopus 로고
    • Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic di-GMP levels, and enhanced dispersal
    • Barraud, N., Schleheck, D., Klebensberger, J., Webb, J. S., Hassett, D. J., Rice, S. A., and Kjelleberg, S. (2009) Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic di-GMP levels, and enhanced dispersal J. Bacteriol. 191 (23) 7333-7342
    • (2009) J. Bacteriol. , vol.191 , Issue.23 , pp. 7333-7342
    • Barraud, N.1    Schleheck, D.2    Klebensberger, J.3    Webb, J.S.4    Hassett, D.J.5    Rice, S.A.6    Kjelleberg, S.7
  • 18
    • 78650396058 scopus 로고    scopus 로고
    • Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-di-GMP phosphodiesterase with a putative hypoxia-sensing domain
    • An, S., Wu, J., and Zhang, L. H. (2010) Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-di-GMP phosphodiesterase with a putative hypoxia-sensing domain Appl. Environ. Microbiol. 76 (24) 8160-8173
    • (2010) Appl. Environ. Microbiol. , vol.76 , Issue.24 , pp. 8160-8173
    • An, S.1    Wu, J.2    Zhang, L.H.3
  • 19
    • 79851486240 scopus 로고    scopus 로고
    • Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis
    • Yukl, E. T., Ioanoviciu, A., Sivaramakrishnan, S., Nakano, M. M., Ortiz de Montellano, P. R., and Moenne-Loccoz, P. (2011) Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis Biochemistry 50 (6) 1023-1028
    • (2011) Biochemistry , vol.50 , Issue.6 , pp. 1023-1028
    • Yukl, E.T.1    Ioanoviciu, A.2    Sivaramakrishnan, S.3    Nakano, M.M.4    Ortiz De Montellano, P.R.5    Moenne-Loccoz, P.6
  • 20
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • Boon, E. M. and Marletta, M. A. (2005) Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins Curr. Opin. Chem. Biol. 9 (5) 441-446
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.5 , pp. 441-446
    • Boon, E.M.1    Marletta, M.A.2
  • 21
    • 84860666649 scopus 로고    scopus 로고
    • Nitric oxide regulated two-component signaling in Pseudoalteromonas atlantica
    • Arora, D. P. and Boon, E. M. (2012) Nitric oxide regulated two-component signaling in Pseudoalteromonas atlantica Biochem. Biophys. Res. Commun. 421 (3) 521-526
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , Issue.3 , pp. 521-526
    • Arora, D.P.1    Boon, E.M.2
  • 22
    • 79952010744 scopus 로고    scopus 로고
    • Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities
    • Liu, N., Pak, T., and Boon, E. M. (2010) Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities Mol. BioSyst. 6 (9) 1561-1564
    • (2010) Mol. BioSyst. , vol.6 , Issue.9 , pp. 1561-1564
    • Liu, N.1    Pak, T.2    Boon, E.M.3
  • 23
    • 77955401388 scopus 로고    scopus 로고
    • H-NOX regulation of c-di-GMP metabolism and biofilm formation in Legionella pneumophila
    • Carlson, H. K., Vance, R. E., and Marletta, M. A. (2010) H-NOX regulation of c-di-GMP metabolism and biofilm formation in Legionella pneumophila Mol. Microbiol. 77 (4) 930-942
    • (2010) Mol. Microbiol. , vol.77 , Issue.4 , pp. 930-942
    • Carlson, H.K.1    Vance, R.E.2    Marletta, M.A.3
  • 24
    • 84863229664 scopus 로고    scopus 로고
    • Nitric oxide regulation of cyclic di-GMP synthesis and hydrolysis in Shewanella woodyi
    • Liu, N., Xu, Y., Hossain, S., Huang, N., Coursolle, D., Gralnick, J. A., and Boon, E. M. (2010) Nitric oxide regulation of cyclic di-GMP synthesis and hydrolysis in Shewanella woodyi Biochemistry 51 (10) 2087-2099
    • (2010) Biochemistry , vol.51 , Issue.10 , pp. 2087-2099
    • Liu, N.1    Xu, Y.2    Hossain, S.3    Huang, N.4    Coursolle, D.5    Gralnick, J.A.6    Boon, E.M.7
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 73949099815 scopus 로고    scopus 로고
    • A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation
    • Erbil, W. K., Price, M. S., Wemmer, D. E., and Marletta, M. A. (2009) A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation Proc. Natl. Acad. Sci. U.S.A. 106 (47) 19753-19760
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.47 , pp. 19753-19760
    • Erbil, W.K.1    Price, M.S.2    Wemmer, D.E.3    Marletta, M.A.4
  • 27
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Bax, A.2
  • 28
    • 84871444338 scopus 로고    scopus 로고
    • University of Calfornia, San Francisco.
    • Goddard, T. D. and Kneller, D. G. (2008) SPARKY 3, University of Calfornia, San Francisco.
    • (2008) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 29
    • 0034009520 scopus 로고    scopus 로고
    • Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
    • Schuck, P. (2000) Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 30
    • 33746817480 scopus 로고    scopus 로고
    • Nitric oxide binding to prokaryotic homologs of the soluble guanylate cyclase β1 H-NOX domain
    • Boon, E. M., Davis, J. H., Tran, R., Karow, D. S., Huang, S. H., Pan, D., Miazgowicz, M. M., and Marletta, M. A. (2006) Nitric oxide binding to prokaryotic homologs of the soluble guanylate cyclase β1 H-NOX domain J. Biol. Chem. 281 (31) 21892-21902
    • (2006) J. Biol. Chem. , vol.281 , Issue.31 , pp. 21892-21902
    • Boon, E.M.1    Davis, J.H.2    Tran, R.3    Karow, D.S.4    Huang, S.H.5    Pan, D.6    Miazgowicz, M.M.7    Marletta, M.A.8
  • 31
    • 35449002345 scopus 로고    scopus 로고
    • Analytical Ultracentrifugation: Sedimentation Velocity and Sedimentation Equilibrium
    • Cole, J. L., Lary, J. W., Moody, T., and Laue, T. M. (2008) Analytical Ultracentrifugation: Sedimentation Velocity and Sedimentation Equilibrium Methods Cell Biol. 84, 143-179
    • (2008) Methods Cell Biol. , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.3    Laue, T.M.4
  • 32
    • 34247202706 scopus 로고    scopus 로고
    • The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain
    • Malone, J. G., Williams, R., Christen, M., Jenla, U., Spiers, A. J., and Rainey, P. B. (2007) The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain Microbiology 153 (Part 4) 980-994
    • (2007) Microbiology , vol.153 , Issue.PART 4 , pp. 980-994
    • Malone, J.G.1    Williams, R.2    Christen, M.3    Jenla, U.4    Spiers, A.J.5    Rainey, P.B.6
  • 33
    • 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., and Jenal, U. (2007) Activation of the Diguanylate Cyclase PleD by Phosphorylation-mediated Dimerization J. Biol. Chem. 282 (40) 29170-29177
    • (2007) J. Biol. Chem. , vol.282 , Issue.40 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 36
    • 0030561461 scopus 로고    scopus 로고
    • A Spectrophotometric Method to Measure Enzymatic Activity in Reactions That Generate Inorganic Pyrophosphate
    • Upson, R. H., Haugland, R. P., Malekzadeh, M. N., and Haugland, R. P. (1996) A Spectrophotometric Method to Measure Enzymatic Activity in Reactions That Generate Inorganic Pyrophosphate Anal. Biochem. 243 (1) 41-45
    • (1996) Anal. Biochem. , vol.243 , Issue.1 , pp. 41-45
    • Upson, R.H.1    Haugland, R.P.2    Malekzadeh, M.N.3    Haugland, R.P.4
  • 37
    • 0020681165 scopus 로고
    • Inorganic phosphate assay with malachite green: An improvement and evaluation
    • Carter, S. G. and Karl, D. W. (1982) Inorganic phosphate assay with malachite green: An improvement and evaluation J. Biochem. Biophys. Methods 7 (1) 7-13
    • (1982) J. Biochem. Biophys. Methods , vol.7 , Issue.1 , pp. 7-13
    • Carter, S.G.1    Karl, D.W.2
  • 38
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: Mechanisms of signalling
    • Mills, E., Pultz, I. S., Kulasekara, H. D., and Miller, S. I. (2011) The bacterial second messenger c-di-GMP: Mechanisms of signalling Cell. Microbiol. 13 (8) 1122-1129
    • (2011) Cell. Microbiol. , vol.13 , Issue.8 , pp. 1122-1129
    • Mills, E.1    Pultz, I.S.2    Kulasekara, H.D.3    Miller, S.I.4
  • 39
    • 84862527194 scopus 로고    scopus 로고
    • Sensing the messenger: The diverse ways that bacteria signal through c-di-GMP
    • Krasteva, P. V., Giglio, K. M., and Sondermann, H. (2012) Sensing the messenger: The diverse ways that bacteria signal through c-di-GMP Protein Sci. 21 (7) 929-948
    • (2012) Protein Sci. , vol.21 , Issue.7 , pp. 929-948
    • Krasteva, P.V.1    Giglio, K.M.2    Sondermann, H.3
  • 40
    • 83855165110 scopus 로고    scopus 로고
    • Should we stay or should we go: Mechanisms and ecological consequences for biofilm dispersal
    • McDougald, D., Rice, S. A., Barraud, N., Steinberg, P. D., and Kjelleberg, S. (2012) Should we stay or should we go: Mechanisms and ecological consequences for biofilm dispersal Nat. Rev. Microbiol. 10 (1) 39-50
    • (2012) Nat. Rev. Microbiol. , vol.10 , Issue.1 , pp. 39-50
    • McDougald, D.1    Rice, S.A.2    Barraud, N.3    Steinberg, P.D.4    Kjelleberg, S.5
  • 41
    • 33846491964 scopus 로고    scopus 로고
    • NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism
    • Ma, X., Sayed, N., Beuve, A., and van den Akker, F. (2007) NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism EMBO J. 26, 578-588
    • (2007) EMBO J. , vol.26 , pp. 578-588
    • Ma, X.1    Sayed, N.2    Beuve, A.3    Van Den Akker, F.4
  • 42
    • 84876841559 scopus 로고    scopus 로고
    • Higher-order interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase
    • Underbakke, E. S., Iavarone, A. T., and Marletta, M. A. (2013) Higher-order interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase Proc. Natl. Acad. Sci. U.S.A. 110 (17) 6777-6782
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , Issue.17 , pp. 6777-6782
    • Underbakke, E.S.1    Iavarone, A.T.2    Marletta, M.A.3
  • 43
    • 4444333687 scopus 로고    scopus 로고
    • Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases
    • Pellicena, P., Karow, D. S., Boon, E. M., Marletta, M. A., and Kuriyan, J. (2004) Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases Proc. Natl. Acad. Sci. U.S.A. 101 (35) 12854-12859
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.35 , pp. 12854-12859
    • Pellicena, P.1    Karow, D.S.2    Boon, E.M.3    Marletta, M.A.4    Kuriyan, J.5
  • 44
    • 58149173292 scopus 로고    scopus 로고
    • Probing the function of heme distortion in the H-NOX family
    • Olea, C., Boon, E. M., Pellicna, P., Kuriyan, J., and Marletta, M. A. (2008) Probing the function of heme distortion in the H-NOX family ACS Chem. Biol. 3 (11) 703-710
    • (2008) ACS Chem. Biol. , vol.3 , Issue.11 , pp. 703-710
    • Olea, C.1    Boon, E.M.2    Pellicna, P.3    Kuriyan, J.4    Marletta, M.A.5
  • 45
    • 84856472302 scopus 로고    scopus 로고
    • Heme flattening is sufficient for signal transduction in the H-NOX family
    • Muralidharan, S. and Boon, E. M. (2012) Heme flattening is sufficient for signal transduction in the H-NOX family J. Am. Chem. Soc. 134 (4) 2044-2046
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.4 , pp. 2044-2046
    • Muralidharan, S.1    Boon, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.