메뉴 건너뛰기




Volumn 45, Issue 16, 2017, Pages 9773-9787

Mechanistic insight into how multidrug resistant Acinetobacter baumannii response regulator AdeR recognizes an intercistronic region

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; GLUTATHIONE; LYSINE; MAGNESIUM; PROTEIN ADER; REGULATOR PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; SPACER DNA;

EID: 85031924610     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkx624     Document Type: Article
Times cited : (18)

References (51)
  • 2
    • 42549108748 scopus 로고    scopus 로고
    • Antimicrobial resistance: Acinetobacter baumannii: Epidemiology, antimicrobial resistance, and treatment options
    • Maragakis, L.L. and Perl, T.M. (2008) Antimicrobial resistance: Acinetobacter baumannii: Epidemiology, antimicrobial resistance, and treatment options. Clin. Infect. Dis., 46, 1254-1263.
    • (2008) Clin. Infect. Dis. , vol.46 , pp. 1254-1263
    • Maragakis, L.L.1    Perl, T.M.2
  • 3
    • 84937765381 scopus 로고    scopus 로고
    • Emerging broad-spectrum resistance in Pseudomonas aeruginosa and Acinetobacter baumannii: Mechanisms and epidemiology
    • Potron, A., Poirel, L. and Nordmann, P. (2015) Emerging broad-spectrum resistance in Pseudomonas aeruginosa and Acinetobacter baumannii: mechanisms and epidemiology. Int. J. Antimicrob. Agents, 45, 568-585.
    • (2015) Int. J. Antimicrob. Agents , vol.45 , pp. 568-585
    • Potron, A.1    Poirel, L.2    Nordmann, P.3
  • 4
    • 84867184096 scopus 로고    scopus 로고
    • Adaptive and mutational resistance: Role of porins and efflux pumps in drug resistance
    • Lucia Fernandez, R.E.W.H. (2012) Adaptive and mutational resistance: role of porins and efflux pumps in drug resistance. Clin. Microbiol. Rev., 25, 661-681.
    • (2012) Clin. Microbiol. Rev. , vol.25 , pp. 661-681
    • Lucia Fernandez, R.E.W.H.1
  • 5
    • 84926035587 scopus 로고    scopus 로고
    • The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria
    • Li, X.Z., Plesiat, P. and Nikaido, H. (2015) The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria. Clin. Microbiol. Rev., 28, 337-418.
    • (2015) Clin. Microbiol. Rev. , vol.28 , pp. 337-418
    • Li, X.Z.1    Plesiat, P.2    Nikaido, H.3
  • 6
    • 0035178557 scopus 로고    scopus 로고
    • Resistance-nodulation-cell division-type efflux pump involved in aminoglycoside resistance
    • Magnet, S., Courvalin, P. and Lambert, T. (2001) Resistance-nodulation-cell division-type efflux pump involved in aminoglycoside resistance. Antimicrob. Agents Chemother., 45, 3375-3380.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3375-3380
    • Magnet, S.1    Courvalin, P.2    Lambert, T.3
  • 7
    • 38649116649 scopus 로고    scopus 로고
    • AdeIJK, a resistance-nodulation-cell division pump effluxing multiple antibiotics in Acinetobacter baumannii
    • Damier-Piolle, L., Magnet, S., Brémont, S., Lambert, T. and Courvalin, P. (2008) AdeIJK, a resistance-nodulation-cell division pump effluxing multiple antibiotics in Acinetobacter baumannii. Antimicrob. Agents Chemother., 52, 557-562.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 557-562
    • Damier-Piolle, L.1    Magnet, S.2    Brémont, S.3    Lambert, T.4    Courvalin, P.5
  • 8
    • 77957365300 scopus 로고    scopus 로고
    • Overexpression of resistance-nodulation-cell division pump AdeFGH confers multidrug resistance in Acinetobacter baumannii
    • Coyne, S., Rosenfeld, N., Lambert, T., Courvalin, P. and Périchon, B. (2010) Overexpression of resistance-nodulation-cell division pump AdeFGH confers multidrug resistance in Acinetobacter baumannii. Antimicrob. Agents Chemother., 54, 4389-4393.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4389-4393
    • Coyne, S.1    Rosenfeld, N.2    Lambert, T.3    Courvalin, P.4    Périchon, B.5
  • 9
    • 84890407663 scopus 로고    scopus 로고
    • Decreased susceptibility to tigecycline in acinetobacter baumannii mediated by a mutation in trm encoding SAM-dependent methyltransferase
    • Chen, Q., Li, X., Zhou, H., Jiang, Y., Chen, Y., Hua, X. and Yu, Y. (2014) Decreased susceptibility to tigecycline in acinetobacter baumannii mediated by a mutation in trm encoding SAM-dependent methyltransferase. J. Antimicrob. Chemother., 69, 72-76.
    • (2014) J. Antimicrob. Chemother. , vol.69 , pp. 72-76
    • Chen, Q.1    Li, X.2    Zhou, H.3    Jiang, Y.4    Chen, Y.5    Hua, X.6    Yu, Y.7
  • 12
    • 85009769722 scopus 로고    scopus 로고
    • Genetic regulation of virulence and antibiotic resistance in Acinetobacter baumannii
    • Kröger, C., Kary, S., Schauer, K. and Cameron, A. (2016) Genetic regulation of virulence and antibiotic resistance in Acinetobacter baumannii. Genes (Basel)., 8, 1-19.
    • (2016) Genes (Basel) , vol.8 , pp. 1-19
    • Kröger, C.1    Kary, S.2    Schauer, K.3    Cameron, A.4
  • 13
    • 84957922086 scopus 로고    scopus 로고
    • The Asp20-to-Asn substitution in the response regulator AdeR leads to enhanced efflux activity of AdeB in Acinetobacter baumannii
    • Nowak, J., Schneiders, T., Seifert, H. and Higgins, P.G. (2016) The Asp20-to-Asn substitution in the response regulator AdeR leads to enhanced efflux activity of AdeB in Acinetobacter baumannii. Antimicrob. Agents Chemother., 60, 1085-1090.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 1085-1090
    • Nowak, J.1    Schneiders, T.2    Seifert, H.3    Higgins, P.G.4
  • 14
    • 84879018937 scopus 로고    scopus 로고
    • RND-type efflux pumps in multidrug-resistant clinical isolates of Acinetobacter baumannii: Major role for AdeABC overexpression and aders mutations
    • Yoon, E.J., Courvalin, P. and Grillot-Courvalin, C. (2013) RND-type efflux pumps in multidrug-resistant clinical isolates of Acinetobacter baumannii: Major role for AdeABC overexpression and aders mutations. Antimicrob. Agents Chemother., 57, 2989-2995.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 2989-2995
    • Yoon, E.J.1    Courvalin, P.2    Grillot-Courvalin, C.3
  • 15
    • 84871016428 scopus 로고    scopus 로고
    • The evolution of two-component signal transduction systems
    • Capra, E.J., Michael and Laub, T. (2012) The evolution of two-component signal transduction systems. Annu. Rev. Microbiol., 66, 325-347.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 325-347
    • Capra, E.J.1    Michael2    Laub, T.3
  • 16
    • 77949916499 scopus 로고    scopus 로고
    • Two-component signal transduction as potential drug targets in pathogenic bacteria
    • Gotoh, Y., Eguchi, Y., Watanabe, T., Okamoto, S., Doi, A. and Utsumi, R. (2010) Two-component signal transduction as potential drug targets in pathogenic bacteria. Curr. Opin. Microbiol., 13, 232-239.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 232-239
    • Gotoh, Y.1    Eguchi, Y.2    Watanabe, T.3    Okamoto, S.4    Doi, A.5    Utsumi, R.6
  • 17
    • 84986540400 scopus 로고    scopus 로고
    • Feedback control of two-component regulatory systems
    • Groisman, E.A. (2016) Feedback control of two-component regulatory systems. Annu. Rev. Microbiol., 70, 103-124.
    • (2016) Annu. Rev. Microbiol. , vol.70 , pp. 103-124
    • Groisman, E.A.1
  • 18
    • 34248205790 scopus 로고    scopus 로고
    • Bacterial response regulators: Versatile regulatory strategies from common domains
    • Gao, R., Mack, T.R. and Stock, A.M. (2007) Bacterial response regulators: versatile regulatory strategies from common domains. Trends Biochem. Sci., 32, 225-234.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 225-234
    • Gao, R.1    Mack, T.R.2    Stock, A.M.3
  • 19
    • 84965161649 scopus 로고    scopus 로고
    • The Acinetobacter baumannii two-component system aders regulates genes required for multidrug efflux, biofilm formation, and virulence in a strain-specific manner
    • Richmond, G.E., Evans, L.P., Anderson, M.J., Wand, M.E., Bonney, L.C., Ivens, A., Chua, K.L., Webber, M.A., Mark Sutton, J., Peterson, M.L. et al. (2016) The Acinetobacter baumannii two-component system aders regulates genes required for multidrug efflux, biofilm formation, and virulence in a strain-specific manner. MBio, 7, 1-12.
    • (2016) MBio , vol.7 , pp. 1-12
    • Richmond, G.E.1    Evans, L.P.2    Anderson, M.J.3    Wand, M.E.4    Bonney, L.C.5    Ivens, A.6    Chua, K.L.7    Webber, M.A.8    Mark Sutton, J.9    Peterson, M.L.10
  • 20
    • 55949126211 scopus 로고    scopus 로고
    • Inhibitors targeting two-component signal transduction
    • Watanabe, T., Okada, A., Gotoh, Y. and Utsumi, R. (2008) Inhibitors targeting two-component signal transduction. Adv Exp Med Biol, 631, 229-236.
    • (2008) Adv Exp Med Biol , vol.631 , pp. 229-236
    • Watanabe, T.1    Okada, A.2    Gotoh, Y.3    Utsumi, R.4
  • 22
    • 84986601850 scopus 로고    scopus 로고
    • Molecular mechanisms of two-component signal transduction
    • Zschiedrich, C.P., Keidel, V. and Szurmant, H. (2016) Molecular mechanisms of two-component signal transduction. J. Mol. Biol., 428, 3752-3775.
    • (2016) J. Mol. Biol. , vol.428 , pp. 3752-3775
    • Zschiedrich, C.P.1    Keidel, V.2    Szurmant, H.3
  • 23
    • 84957057136 scopus 로고    scopus 로고
    • AdeR protein regulates adeABC expression by binding to a direct-repeat motif in the intercistronic spacer
    • Chang, T.Y., Huang, B.J., Sun, J.R., Perng, C.L., Chan, M.C., Yu, C.P. and Chiueh, T.S. (2016) AdeR protein regulates adeABC expression by binding to a direct-repeat motif in the intercistronic spacer. Microbiol. Res., 183, 60-67.
    • (2016) Microbiol. Res. , vol.183 , pp. 60-67
    • Chang, T.Y.1    Huang, B.J.2    Sun, J.R.3    Perng, C.L.4    Chan, M.C.5    Yu, C.P.6    Chiueh, T.S.7
  • 24
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng, L., Baumann, U. and Reymond, J.-L. (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res., 32, e115.
    • (2004) Nucleic Acids Res. , vol.32 , pp. e115
    • Zheng, L.1    Baumann, U.2    Reymond, J.-L.3
  • 27
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A.J. (2006) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. Sect. D Biol. Crystallogr., 63, 32-41.
    • (2006) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 29
    • 53049099975 scopus 로고    scopus 로고
    • Response regulator YycF essential for bacterial growth: X-ray crystal structure of the DNA-binding domain and its PhoB-like DNA recognition motif
    • Okajima, T., Doi, A., Okada, A., Gotoh, Y., Tanizawa, K. and Utsumi, R. (2008) Response regulator YycF essential for bacterial growth: X-ray crystal structure of the DNA-binding domain and its PhoB-like DNA recognition motif. FEBS Lett., 582, 3434-3438.
    • (2008) FEBS Lett. , vol.582 , pp. 3434-3438
    • Okajima, T.1    Doi, A.2    Okada, A.3    Gotoh, Y.4    Tanizawa, K.5    Utsumi, R.6
  • 32
    • 84989879289 scopus 로고    scopus 로고
    • The new NCPSS BL19U2 beamline at the SSRF for small-Angle X-ray scattering from biological macromolecules in solution
    • Li, N., Li, X., Wang, Y., Liu, G., Zhou, P., Wu, H., Hong, C., Bian, F. and Zhang, R. (2016) The new NCPSS BL19U2 beamline at the SSRF for small-Angle X-ray scattering from biological macromolecules in solution. J. Appl. Crystallogr., 49, 1428-1432.
    • (2016) J. Appl. Crystallogr. , vol.49 , pp. 1428-1432
    • Li, N.1    Li, X.2    Wang, Y.3    Liu, G.4    Zhou, P.5    Wu, H.6    Hong, C.7    Bian, F.8    Zhang, R.9
  • 33
    • 84922709449 scopus 로고    scopus 로고
    • The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence
    • Wen, Y., Behiels, E., Felix, J., Elegheert, J., Vergauwen, B., Devreese, B. and Savvides, S.N. (2014) The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence. Nucleic Acids Res., 42, 10134-10147.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 10134-10147
    • Wen, Y.1    Behiels, E.2    Felix, J.3    Elegheert, J.4    Vergauwen, B.5    Devreese, B.6    Savvides, S.N.7
  • 34
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D.I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr., 25, 495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 36
    • 0029185933 scopus 로고
    • CRYSOL-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C. and Koch, M.H.J. (1995) CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 37
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • Fischer, H., De Oliveira Neto, M., Napolitano, H.B., Polikarpov, I. and Craievich, A.F. (2010) Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. J. Appl. Crystallogr., 43, 101-109.
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliveira-Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 38
    • 0031574026 scopus 로고    scopus 로고
    • NUCPLOT: A program to generate schematic diagrams of protein-nucleic acid interactions
    • Luscombe, N.M., Laskowski, R.A. and Thornton, J.M. (1997) NUCPLOT: a program to generate schematic diagrams of protein-nucleic acid interactions. Nucleic Acids Res., 25, 4940-4945.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4940-4945
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 39
    • 1342346615 scopus 로고    scopus 로고
    • Residues required for Bacillus subtilis PhoP DNA binding or RNA polymerase interaction: Alanine scanning of PhoP effector domain transactivation loop and Helix 3
    • Chen, Y., Abdel-fattah, W.R. and Hulett, F.M. (2004) Residues required for Bacillus subtilis PhoP DNA binding or RNA polymerase interaction: alanine scanning of PhoP effector domain transactivation loop and Helix 3. J. Bacteriol., 186, 1493-1502.
    • (2004) J. Bacteriol. , vol.186 , pp. 1493-1502
    • Chen, Y.1    Abdel-Fattah, W.R.2    Hulett, F.M.3
  • 40
    • 0035902464 scopus 로고    scopus 로고
    • BeF (3) (-) acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF (3) (-) complex with phosphoserine phosphatase
    • Cho, H., Wang, W., Kim, R., Yokota, H., Damo, S., Kim, S.H., Wemmer, D., Kustu, S. and Yan, D. (2001) BeF (3) (-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF (3) (-) complex with phosphoserine phosphatase. Proc. Natl. Acad. Sci. U.S.A., 98, 8525-8530.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8525-8530
    • Cho, H.1    Wang, W.2    Kim, R.3    Yokota, H.4    Damo, S.5    Kim, S.H.6    Wemmer, D.7    Kustu, S.8    Yan, D.9
  • 41
    • 84878143682 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation
    • Leonard, P.G., Golemi-Kotra, D. and Stock, A.M. (2013) Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation. Proc. Natl. Acad. Sci. U.S.A., 110, 8525-8530.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8525-8530
    • Leonard, P.G.1    Golemi-Kotra, D.2    Stock, A.M.3
  • 44
    • 34547104863 scopus 로고    scopus 로고
    • Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism
    • Hong, E., Lee, H.M., Ko, H., Kim, D., Jeon, B., Jung, J., Shin, J., Lee, S., Kim, Y., Jeon, Y.H. et al. (2007) Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism. J. Biol. Chem., 282, 20667-20675.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20667-20675
    • Hong, E.1    Lee, H.M.2    Ko, H.3    Kim, D.4    Jeon, B.5    Jung, J.6    Shin, J.7    Lee, S.8    Kim, Y.9    Jeon, Y.H.10
  • 45
    • 77949880884 scopus 로고    scopus 로고
    • Receiver domain structure and function in response regulator proteins
    • Bourret, R.B. (2010) Receiver domain structure and function in response regulator proteins. Curr. Opin. Microbiol., 13, 142-149.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 142-149
    • Bourret, R.B.1
  • 46
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino, P., Rubio, V. and Marina, A. (2009) Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell, 139, 325-336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 47
    • 34547743126 scopus 로고    scopus 로고
    • Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofiuoride
    • Bachhawat, P. and Stock, A.M. (2007) Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofiuoride. J. Bacteriol., 189, 5987-5995.
    • (2007) J. Bacteriol. , vol.189 , pp. 5987-5995
    • Bachhawat, P.1    Stock, A.M.2
  • 49
    • 84856708226 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl
    • Dou, H., Buetow, L., Hock, A., Sibbet, G.J., Vousden, K.H. and Huang, D.T. (2012) Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nat. Struct. Mol. Biol., 19, 184-192.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 184-192
    • Dou, H.1    Buetow, L.2    Hock, A.3    Sibbet, G.J.4    Vousden, K.H.5    Huang, D.T.6
  • 50
    • 78649667671 scopus 로고    scopus 로고
    • In vivo selection of a missense mutation in adeR and conversion of the novel blaOXA-164 gene into blaOXA-58in carbapenem-resistant Acinetobacter baumannii isolates from a hospitalized patient
    • Higgins, P.G., Schneiders, T., Hamprecht, A. and Seifert, H. (2010) In vivo selection of a missense mutation in adeR and conversion of the novel blaOXA-164 gene into blaOXA-58in carbapenem-resistant Acinetobacter baumannii isolates from a hospitalized patient. Antimicrob. Agents Chemother., 54, 5021-5027.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 5021-5027
    • Higgins, P.G.1    Schneiders, T.2    Hamprecht, A.3    Seifert, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.