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Volumn 196, Issue 22, 2014, Pages 3890-3902

Structural and functional characterization of Pseudomonas aeruginosa global regulator AmpR

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BETA GALACTOSIDASE; BETA LACTAMASE; BETA LACTAMASE AMPC; BETA LACTAMASE AMPR; UNCLASSIFIED DRUG; AMPC BETA-LACTAMASES; AMPR PROTEIN, BACTERIA; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; BETA LACTAM; PROTEIN BINDING;

EID: 84917708881     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01997-14     Document Type: Article
Times cited : (37)

References (87)
  • 1
    • 0027404779 scopus 로고
    • Pathogenesis of cystic fibrosis
    • Koch C, Hoiby N. 1993. Pathogenesis of cystic fibrosis. Lancet 341:1065-1069. http://dx.doi.org/10.1016/0140-6736(93)92422-P.
    • (1993) Lancet , vol.341 , pp. 1065-1069
    • Koch, C.1    Hoiby, N.2
  • 2
    • 0028789107 scopus 로고
    • Mechanisms of resistance to β-lactam antibiotics amongst Pseudomonas aeruginosa isolates collected in the UK in 1993
    • Chen HY, Yuan M, Livermore DM. 1995. Mechanisms of resistance to β-lactam antibiotics amongst Pseudomonas aeruginosa isolates collected in the UK in 1993. J. Med. Microbiol. 43:300-309. http://dx.doi.org/10.1099/00222615-43-4-300.
    • (1995) J. Med. Microbiol. , vol.43 , pp. 300-309
    • Chen, H.Y.1    Yuan, M.2    Livermore, D.M.3
  • 5
    • 0025061590 scopus 로고
    • Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed β-lactamase producing strains
    • Giwercman B, Lambert PA, Rosdahl VT, Shand GH, Hoiby N. 1990. Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed β-lactamase producing strains. J. Antimicrob. Chemother. 26:247-259. http://dx.doi.org/10.1093/jac/26.2.247.
    • (1990) J. Antimicrob. Chemother. , vol.26 , pp. 247-259
    • Giwercman, B.1    Lambert, P.A.2    Rosdahl, V.T.3    Shand, G.H.4    Hoiby, N.5
  • 6
    • 0026501586 scopus 로고
    • High-level β-lactamase activity in sputum samples from cystic fibrosis patients during antipseudomonal treatment
    • Giwercman B, Meyer C, Lambert PA, Reinert C, Hoiby N. 1992. High-level β-lactamase activity in sputum samples from cystic fibrosis patients during antipseudomonal treatment. Antimicrob. Agents Chemother. 36:71-76. http://dx.doi.org/10.1128/AAC.36.1.71.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 71-76
    • Giwercman, B.1    Meyer, C.2    Lambert, P.A.3    Reinert, C.4    Hoiby, N.5
  • 7
    • 27644573842 scopus 로고    scopus 로고
    • Molecular mechanisms of β-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains
    • Juan C, Macia MD, Gutierrez O, Vidal C, Perez JL, Oliver A. 2005. Molecular mechanisms of β-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 49:4733-4738. http://dx.doi.org/10.1128/AAC.49.11.4733-4738.2005.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4733-4738
    • Juan, C.1    Macia, M.D.2    Gutierrez, O.3    Vidal, C.4    Perez, J.L.5    Oliver, A.6
  • 8
    • 0032700851 scopus 로고    scopus 로고
    • Regulation of inducible AmpC β-lactamase expression among Enterobacteriaceae
    • Hanson ND, Sanders CC. 1999. Regulation of inducible AmpC β-lactamase expression among Enterobacteriaceae. Curr. Pharm. Des. 5:881-894.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 881-894
    • Hanson, N.D.1    Sanders, C.C.2
  • 9
    • 0014155877 scopus 로고
    • Inducible β-lactamase in Enterobacter
    • Hennessey TD. 1967. Inducible β-lactamase in Enterobacter. J. Gen. Microbiol. 49:277-285. http://dx.doi.org/10.1099/00221287-49-2-277.
    • (1967) J. Gen. Microbiol. , vol.49 , pp. 277-285
    • Hennessey, T.D.1
  • 10
    • 0000297348 scopus 로고
    • Contribution of chromosomal β-lactamases to β-lactam resistance in enterobacteria
    • Lindberg F, Normark S. 1986. Contribution of chromosomal β-lactamases to β-lactam resistance in enterobacteria. Rev. Infect. Dis. 8(Suppl 3): S292-S304. http://dx.doi.org/10.1093/clinids/8.Supplement_3.S292.
    • (1986) Rev. Infect. Dis. , vol.8 , pp. S292-S304
    • Lindberg, F.1    Normark, S.2
  • 12
    • 0023054166 scopus 로고
    • Inducible cephalosporinase production in clinical isolates of Enterobacter cloacae is controlled by a regulatory gene that has been deleted from Escherichia coli
    • Honore N, Nicolas MH, Cole ST. 1986. Inducible cephalosporinase production in clinical isolates of Enterobacter cloacae is controlled by a regulatory gene that has been deleted from Escherichia coli. EMBO J. 5:3709-3714.
    • (1986) EMBO J. , vol.5 , pp. 3709-3714
    • Honore, N.1    Nicolas, M.H.2    Cole, S.T.3
  • 13
    • 0023134051 scopus 로고
    • Common mechanism of ampC β-lactamase induction in enterobacteria: regulation of the cloned Enterobacter cloacae P99 β-lactamase gene
    • Lindberg F, Normark S. 1987. Common mechanism of ampC β-lactamase induction in enterobacteria: regulation of the cloned Enterobacter cloacae P99 β-lactamase gene. J. Bacteriol. 169:758-763.
    • (1987) J. Bacteriol. , vol.169 , pp. 758-763
    • Lindberg, F.1    Normark, S.2
  • 14
    • 0000623780 scopus 로고
    • Regulatory components in Citrobacter freundii ampC β-lactamase induction
    • Lindberg F, Westman L, Normark S. 1985. Regulatory components in Citrobacter freundii ampC β-lactamase induction. Proc. Natl. Acad. Sci. U. S. A. 82:4620-4624. http://dx.doi.org/10.1073/pnas.82.14.4620.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4620-4624
    • Lindberg, F.1    Westman, L.2    Normark, S.3
  • 15
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks SE, Oyston PC. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-3623. http://dx.doi.org/10.1099/mic.0.2008/022772-0.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 16
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell MA. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626. http://dx.doi.org/10.1146/annurev.mi.47.100193.003121.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 17
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria
    • Jacobs C, Frere JM, Normark S. 1997. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in Gram-negative bacteria. Cell 88:823-832. http://dx.doi.org/10.1016/S0092-8674(00)81928-5.
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frere, J.M.2    Normark, S.3
  • 18
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs C, Huang LJ, Bartowsky E, Normark S, Park JT. 1994. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction. EMBO J. 13:4684-4694.
    • (1994) EMBO J. , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 19
    • 0029311691 scopus 로고
    • β-Lactamase induction in Gram-negative bacteria is intimately linked to peptidoglycan recycling
    • Normark S. 1995. β-Lactamase induction in Gram-negative bacteria is intimately linked to peptidoglycan recycling. Microb. Drug Resist. 1:111-114. http://dx.doi.org/10.1089/mdr.1995.1.111.
    • (1995) Microb. Drug Resist. , vol.1 , pp. 111-114
    • Normark, S.1
  • 20
    • 0026035965 scopus 로고
    • Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp operon
    • Tuomanen E, Lindquist S, Sande S, Galleni M, Light K, Gage D, Normark S. 1991. Coordinate regulation of β-lactamase induction and peptidoglycan composition by the amp operon. Science 251:201-204. http://dx.doi.org/10.1126/science.1987637.
    • (1991) Science , vol.251 , pp. 201-204
    • Tuomanen, E.1    Lindquist, S.2    Sande, S.3    Galleni, M.4    Light, K.5    Gage, D.6    Normark, S.7
  • 21
    • 0036889483 scopus 로고    scopus 로고
    • Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides
    • Cheng Q, Park JT. 2002. Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J. Bacteriol. 184: 6434-6436. http://dx.doi.org/10.1128/JB.184.23.6434-6436.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 6434-6436
    • Cheng, Q.1    Park, J.T.2
  • 22
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng Q, Li H, Merdek K, Park JT. 2000. Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J. Bacteriol. 182:4836-4840. http://dx.doi.org/10.1128/JB.182.17.4836-4840.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 23
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-Nacetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • Votsch W, Templin MF. 2000. Characterization of a β-Nacetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction. J. Biol. Chem. 275:39032-39038. http://dx.doi.org/10.1074/jbc.M004797200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39032-39038
    • Votsch, W.1    Templin, M.F.2
  • 24
    • 0028168986 scopus 로고
    • The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase
    • Holtje JV, Kopp U, Ursinus A, Wiedemann B. 1994. The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiol. Lett. 122:159-164. http://dx.doi.org/10.1111/j.1574-6968.1994.tb07159.x.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 159-164
    • Holtje, J.V.1    Kopp, U.2    Ursinus, A.3    Wiedemann, B.4
  • 26
    • 0030198727 scopus 로고    scopus 로고
    • The role of N-actylglucosaminyl-1,6 anhydro N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic acid-D-alanine for the induction of β-lactamase in Enterobacter cloacae
    • Dietz H, Wiedemann B. 1996. The role of N-actylglucosaminyl-1,6 anhydro N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic acid-D-alanine for the induction of β-lactamase in Enterobacter cloacae. Zentralbl. Bakteriol. 284:207-217. http://dx.doi.org/10.1016/S0934-8840(96)80096-X.
    • (1996) Zentralbl. Bakteriol. , vol.284 , pp. 207-217
    • Dietz, H.1    Wiedemann, B.2
  • 27
    • 0020458828 scopus 로고
    • Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
    • Mengin-Lecreulx D, Flouret B, van Heijenoort J. 1982. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151:1109-1117.
    • (1982) J. Bacteriol. , vol.151 , pp. 1109-1117
    • Mengin-Lecreulx, D.1    Flouret, B.2    van Heijenoort, J.3
  • 28
    • 0029796071 scopus 로고    scopus 로고
    • Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid, presumed signal molecule for β-lactamase induction, in the bacterial cell
    • Dietz H, Pfeifle D, Wiedemann B. 1996. Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid, presumed signal molecule for β-lactamase induction, in the bacterial cell. Antimicrob. Agents Chemother. 40:2173-2177.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2173-2177
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 29
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramylpentapeptide
    • Dietz H, Pfeifle D, Wiedemann B. 1997. The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramylpentapeptide. Antimicrob. Agents Chemother. 41:2113-2120.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 30
    • 33646458074 scopus 로고    scopus 로고
    • Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring highlevel β-lactam resistance involves three AmpD homologues
    • Juan C, Moya B, Perez JL, Oliver A. 2006. Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring highlevel β-lactam resistance involves three AmpD homologues. Antimicrob. Agents Chemother. 50:1780-1787. http://dx.doi.org/10.1128/AAC.50.5.1780-1787.2006.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1780-1787
    • Juan, C.1    Moya, B.2    Perez, J.L.3    Oliver, A.4
  • 31
    • 27644463418 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors
    • Kong K-F, Jayawardena SR, Indulkar SD, del Puerto A, Koh C-L, Hoiby N, Mathee K. 2005. Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob. Agents Chemother. 49:4567-4575. http://dx.doi.org/10.1128/AAC.49.11.4567-4575.2005.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4567-4575
    • Kong, K.-F.1    Jayawardena, S.R.2    Indulkar, S.D.3    del Puerto, A.4    Koh, C.-L.5    Hoiby, N.6    Mathee, K.7
  • 32
    • 0031760856 scopus 로고    scopus 로고
    • An ampD gene in Pseudomonas aeruginosa encodes a negative regulator of AmpC β-lactamase expression
    • Langaee TY, Dargis M, Huletsky A. 1998. An ampD gene in Pseudomonas aeruginosa encodes a negative regulator of AmpC β-lactamase expression. Antimicrob. Agents Chemother. 42:3296-3300.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 3296-3300
    • Langaee, T.Y.1    Dargis, M.2    Huletsky, A.3
  • 33
    • 0033993765 scopus 로고    scopus 로고
    • Inactivation of the ampD gene in Pseudomonas aeruginosa leads to moderate-basal-level and hyperinducible AmpC β-lactamase expression
    • Langaee TY, Gagnon L, Huletsky A. 2000. Inactivation of the ampD gene in Pseudomonas aeruginosa leads to moderate-basal-level and hyperinducible AmpC β-lactamase expression. Antimicrob. Agents Chemother. 44: 583-589. http://dx.doi.org/10.1128/AAC.44.3.583-589.2000.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 583-589
    • Langaee, T.Y.1    Gagnon, L.2    Huletsky, A.3
  • 34
    • 0027328960 scopus 로고
    • Investigation of the Pseudomonas aeruginosa ampR gene and its role at the chromosomal ampC β-lactamase promoter
    • Lodge J, Busby S, Piddock L. 1993. Investigation of the Pseudomonas aeruginosa ampR gene and its role at the chromosomal ampC β-lactamase promoter. FEMS Microbiol. Lett. 111:315-320. http://dx.doi.org/10.1111/j.1574-6968.1993.tb06404.x.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 315-320
    • Lodge, J.1    Busby, S.2    Piddock, L.3
  • 35
    • 0025600978 scopus 로고
    • Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC β-lactamase
    • Lodge JM, Minchin SD, Piddock LJ, Busby JW. 1990. Cloning, sequencing and analysis of the structural gene and regulatory region of the Pseudomonas aeruginosa chromosomal ampC β-lactamase. Biochem. J. 272: 627-631.
    • (1990) Biochem. J. , vol.272 , pp. 627-631
    • Lodge, J.M.1    Minchin, S.D.2    Piddock, L.J.3    Busby, J.W.4
  • 37
    • 79955534986 scopus 로고    scopus 로고
    • AmpG inactivation restores susceptibility of pan-β-lactam-resistant Pseudomonas aeruginosa clinical strains
    • Zamorano L, Reeve TM, Juan C, Moya B, Cabot G, Vocadlo DJ, Mark BL, Oliver A. 2011. AmpG inactivation restores susceptibility of pan-β-lactam-resistant Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 55:1990-1996. http://dx.doi.org/10.1128/AAC.01688-10.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 1990-1996
    • Zamorano, L.1    Reeve, T.M.2    Juan, C.3    Moya, B.4    Cabot, G.5    Vocadlo, D.J.6    Mark, B.L.7    Oliver, A.8
  • 38
    • 78650628952 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpP
    • Kong KF, Aguila A, Schneper L, Mathee K. 2010. Pseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpP. BMC Microbiol. 10:328. http://dx.doi.org/10.1186/1471-2180-10-328.
    • (2010) BMC Microbiol. , vol.10 , pp. 328
    • Kong, K.F.1    Aguila, A.2    Schneper, L.3    Mathee, K.4
  • 39
    • 84871787592 scopus 로고    scopus 로고
    • A dynamic and intricate regulatory network determines Pseudomonas aeruginosa virulence
    • Balasubramanian D, Schneper L, Kumari H, Mathee K. 2013. A dynamic and intricate regulatory network determines Pseudomonas aeruginosa virulence. Nucleic Acids Res. 41:1-20. http://dx.doi.org/10.1093/nar/gks1039.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1-20
    • Balasubramanian, D.1    Schneper, L.2    Kumari, H.3    Mathee, K.4
  • 40
    • 84859032202 scopus 로고    scopus 로고
    • The regulatory repertoire of Pseudomonas aeruginosa AmpC β-lactamase regulator AmpR includes virulence genes
    • Balasubramanian D, Schneper L, Merighi M, Smith R, Narasimhan G, Lory S, Mathee K. 2012. The regulatory repertoire of Pseudomonas aeruginosa AmpC β-lactamase regulator AmpR includes virulence genes. PLoS One 7:e34067. http://dx.doi.org/10.1371/journal.pone.0034067.
    • (2012) PLoS One , vol.7
    • Balasubramanian, D.1    Schneper, L.2    Merighi, M.3    Smith, R.4    Narasimhan, G.5    Lory, S.6    Mathee, K.7
  • 41
    • 84890814709 scopus 로고    scopus 로고
    • LTQ-XL mass spectrometry proteome analysis expands the Pseudomonas aeruginosa AmpR regulon to include cyclic di-GMP phosphodiesterases and phosphoproteins, and identifies novel open reading frames
    • Kumari H, Murugapiran SK, Balasubramanian D, Schneper L, Merighi M, Sarracino D, Lory S, Mathee K. 2014. LTQ-XL mass spectrometry proteome analysis expands the Pseudomonas aeruginosa AmpR regulon to include cyclic di-GMP phosphodiesterases and phosphoproteins, and identifies novel open reading frames. J. Proteomics 96:328-342. http://dx.doi.org/10.1016/j.jprot.2013.11.018.
    • (2014) J. Proteomics , vol.96 , pp. 328-342
    • Kumari, H.1    Murugapiran, S.K.2    Balasubramanian, D.3    Schneper, L.4    Merighi, M.5    Sarracino, D.6    Lory, S.7    Mathee, K.8
  • 42
    • 84897836308 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa AmpR on β-lactam and non-β-lactam transient cross-resistance upon pre-exposure to subinhibitory concentrations of antibiotics
    • Kumari H, Balasubramanian D, Zincke D, Mathee K. 2014. Role of Pseudomonas aeruginosa AmpR on β-lactam and non-β-lactam transient cross-resistance upon pre-exposure to subinhibitory concentrations of antibiotics. J. Med. Microbiol. 63:544-555. http://dx.doi.org/10.1099/jmm.0.070185-0.
    • (2014) J. Med. Microbiol. , vol.63 , pp. 544-555
    • Kumari, H.1    Balasubramanian, D.2    Zincke, D.3    Mathee, K.4
  • 43
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Furste JP, Pansegrau W, Frank R, Blocker H, Scholz P, Bagdasarian M, Lanka E. 1986. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48:119-131. http://dx.doi.org/10.1016/0378-1119(86)90358-6.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 44
    • 34548850026 scopus 로고    scopus 로고
    • 5 end cDNA amplification using classic RACE
    • Scotto-Lavino E, Du G, Frohman MA. 2006. 5 end cDNA amplification using classic RACE. Nat. Protoc. 1:2555-2562. http://dx.doi.org/10.1038/nprot.2006.480.
    • (2006) Nat. Protoc. , vol.1 , pp. 2555-2562
    • Scotto-Lavino, E.1    Du, G.2    Frohman, M.A.3
  • 45
    • 65349160904 scopus 로고    scopus 로고
    • Determination of the regulon and identification of novelmRNAtargets of Pseudomonas aeruginosa RsmA
    • Brencic A, Lory S. 2009. Determination of the regulon and identification of novelmRNAtargets of Pseudomonas aeruginosa RsmA. Mol. Microbiol. 72:612-632. http://dx.doi.org/10.1111/j.1365-2958.2009.06670.x.
    • (2009) Mol. Microbiol. , vol.72 , pp. 612-632
    • Brencic, A.1    Lory, S.2
  • 46
    • 57749113200 scopus 로고    scopus 로고
    • H-NS family members function coordinately in an opportunistic pathogen
    • Castang S, McManus HR, Turner KH, Dove SL. 2008. H-NS family members function coordinately in an opportunistic pathogen. Proc. Natl. Acad. Sci. U. S. A. 105:18947-18952. http://dx.doi.org/10.1073/pnas.0808215105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18947-18952
    • Castang, S.1    McManus, H.R.2    Turner, K.H.3    Dove, S.L.4
  • 47
    • 33745512838 scopus 로고    scopus 로고
    • A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis
    • Campo N, Rudner DZ. 2006. A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis. Mol. Cell 23:25-35. http://dx.doi.org/10.1016/j.molcel.2006.05.019.
    • (2006) Mol. Cell , vol.23 , pp. 25-35
    • Campo, N.1    Rudner, D.Z.2
  • 49
    • 0030908719 scopus 로고    scopus 로고
    • Posttranslational control of the algT (algU)-encoded σ22 for expression of the alginate regulon in Pseudomonas aeruginosa and localization of its antagonist proteins MucA and MucB (AlgN)
    • Mathee K, McPherson CJ, Ohman DE. 1997. Posttranslational control of the algT (algU)-encoded σ22 for expression of the alginate regulon in Pseudomonas aeruginosa and localization of its antagonist proteins MucA and MucB (AlgN). J. Bacteriol. 179:3711-3720.
    • (1997) J. Bacteriol. , vol.179 , pp. 3711-3720
    • Mathee, K.1    McPherson, C.J.2    Ohman, D.E.3
  • 50
    • 0034937029 scopus 로고    scopus 로고
    • Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli
    • Blank TE, Donnenberg MS. 2001. Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli. J. Bacteriol. 183:4435-4450. http://dx.doi.org/10.1128/JB.183.15.4435-4450.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 4435-4450
    • Blank, T.E.1    Donnenberg, M.S.2
  • 51
    • 0024401346 scopus 로고
    • Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC β-lactamase gene
    • Lindquist S, Lindberg F, Normark S. 1989. Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC β-lactamase gene. J. Bacteriol. 171:3746-3753.
    • (1989) J. Bacteriol. , vol.171 , pp. 3746-3753
    • Lindquist, S.1    Lindberg, F.2    Normark, S.3
  • 52
    • 0034011319 scopus 로고    scopus 로고
    • Dual regulation of mucoidy in Pseudomonas aeruginosa and sigma factor antagonism
    • Boucher JC, Schurr MJ, Deretic V. 2000. Dual regulation of mucoidy in Pseudomonas aeruginosa and sigma factor antagonism. Mol. Microbiol. 36:341-351. http://dx.doi.org/10.1046/j.1365-2958.2000.01846.x.
    • (2000) Mol. Microbiol. , vol.36 , pp. 341-351
    • Boucher, J.C.1    Schurr, M.J.2    Deretic, V.3
  • 54
    • 0033968474 scopus 로고    scopus 로고
    • Integrationproficient plasmids for Pseudomonas aeruginosa: site-specific integration and use for engineering of reporter and expression strains
    • Hoang TT, Kutchma AJ, Becher A, Schweizer HP. 2000. Integrationproficient plasmids for Pseudomonas aeruginosa: site-specific integration and use for engineering of reporter and expression strains. Plasmid 43:59-72. http://dx.doi.org/10.1006/plas.1999.1441.
    • (2000) Plasmid , vol.43 , pp. 59-72
    • Hoang, T.T.1    Kutchma, A.J.2    Becher, A.3    Schweizer, H.P.4
  • 55
    • 0036468362 scopus 로고    scopus 로고
    • Prokaryotic transcription regulators: more than just the helix-turn-helix motif
    • Huffman JL, Brennan RG. 2002. Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol. 12:98-106. http://dx.doi.org/10.1016/S0959-440X(02)00295-6.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 98-106
    • Huffman, J.L.1    Brennan, R.G.2
  • 56
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: transcription regulation and beyond
    • Aravind L, Anantharaman V, Balaji S, Babu MM, Iyer LM. 2005. The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev. 29:231-262. http://dx.doi.org/10.1016/j.femsre.2004.12.008.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5
  • 57
    • 0023681342 scopus 로고
    • Turning λ Cro into a transcriptional activator
    • Bushman FD, Ptashne M. 1988. Turning λ Cro into a transcriptional activator. Cell 54:191-197. http://dx.doi.org/10.1016/0092-8674(88)90551-X.
    • (1988) Cell , vol.54 , pp. 191-197
    • Bushman, F.D.1    Ptashne, M.2
  • 58
    • 0020713848 scopus 로고
    • Repressor structure and the mechanism of positive control
    • Hochschild A, Irwin N, Ptashne M. 1983. Repressor structure and the mechanism of positive control. Cell 32:319-325. http://dx.doi.org/10.1016/0092-8674(83)90451-8.
    • (1983) Cell , vol.32 , pp. 319-325
    • Hochschild, A.1    Irwin, N.2    Ptashne, M.3
  • 59
    • 0031046671 scopus 로고    scopus 로고
    • The activation defect of a λcI positive control mutant
    • Whipple FW, Ptashne M, Hochschild A. 1997. The activation defect of a λcI positive control mutant. J. Mol. Biol. 265:261-265. http://dx.doi.org/10.1006/jmbi.1996.0735.
    • (1997) J. Mol. Biol. , vol.265 , pp. 261-265
    • Whipple, F.W.1    Ptashne, M.2    Hochschild, A.3
  • 60
    • 0024462398 scopus 로고
    • A single glutamic acid residue plays a key role in the transcriptional activation function of λ repressor
    • Bushman FD, Shang C, Ptashne M. 1989. A single glutamic acid residue plays a key role in the transcriptional activation function of λ repressor. Cell 58:1163-1171. http://dx.doi.org/10.1016/0092-8674(89)90514-X.
    • (1989) Cell , vol.58 , pp. 1163-1171
    • Bushman, F.D.1    Shang, C.2    Ptashne, M.3
  • 61
    • 0029813128 scopus 로고    scopus 로고
    • A positive control mutant of the transcription activator protein FIS
    • Gosink KK, Gaal T, Bokal AJ, Gourse RL. 1996. A positive control mutant of the transcription activator protein FIS. J. Bacteriol. 178:5182-5187.
    • (1996) J. Bacteriol. , vol.178 , pp. 5182-5187
    • Gosink, K.K.1    Gaal, T.2    Bokal, A.J.3    Gourse, R.L.4
  • 62
    • 0020329431 scopus 로고
    • Mutant λ phage repressor with a specific defect in its positive control function
    • Guarente L, Nye JS, Hochschild A, Ptashne M. 1982. Mutant λ phage repressor with a specific defect in its positive control function. Proc. Natl. Acad. Sci. U. S. A. 79:2236-2239. http://dx.doi.org/10.1073/pnas.79.7.2236.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2236-2239
    • Guarente, L.1    Nye, J.S.2    Hochschild, A.3    Ptashne, M.4
  • 63
    • 0027161386 scopus 로고
    • Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants ofCAPspecifically defective in transcription activation
    • Zhou Y, Zhang X, Ebright RH. 1993. Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants ofCAPspecifically defective in transcription activation. Proc. Natl. Acad. Sci. U. S. A. 90:6081-6085. http://dx.doi.org/10.1073/pnas.90.13.6081.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 6081-6085
    • Zhou, Y.1    Zhang, X.2    Ebright, R.H.3
  • 64
    • 0025834140 scopus 로고
    • Purification and mutant analysis of Citrobacter freundii AmpR, the regulator for chromosomal AmpC β-lactamase
    • Bartowsky E, Normark S. 1991. Purification and mutant analysis of Citrobacter freundii AmpR, the regulator for chromosomal AmpC β-lactamase. Mol. Microbiol. 5:1715-1725. http://dx.doi.org/10.1111/j.1365-2958.1991.tb01920.x.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1715-1725
    • Bartowsky, E.1    Normark, S.2
  • 65
    • 0027362641 scopus 로고
    • Interactions of wild-type and mutant AmpR of Citrobacter freundii with target DNA
    • Bartowsky E, Normark S. 1993. Interactions of wild-type and mutant AmpR of Citrobacter freundii with target DNA. Mol. Microbiol. 10:555-565. http://dx.doi.org/10.1111/j.1365-2958.1993.tb00927.x.
    • (1993) Mol. Microbiol. , vol.10 , pp. 555-565
    • Bartowsky, E.1    Normark, S.2
  • 66
    • 0033997202 scopus 로고    scopus 로고
    • ampR gene mutations that greatly increase class C β-lactamase activity in Enterobacter cloacae
    • Kuga A, Okamoto R, Inoue M. 2000. ampR gene mutations that greatly increase class C β-lactamase activity in Enterobacter cloacae. Antimicrob. Agents Chemother. 44:561-567. http://dx.doi.org/10.1128/AAC.44.3.561-567.2000.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 561-567
    • Kuga, A.1    Okamoto, R.2    Inoue, M.3
  • 67
    • 0036841078 scopus 로고    scopus 로고
    • Constitutive high expression of chromosomal β-lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampD
    • Bagge N, Ciofu O, Hentzer M, Campbell JI, Givskov M, Hoiby N. 2002. Constitutive high expression of chromosomal β-lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampD. Antimicrob. Agents Chemother. 46:3406-3411. http://dx.doi.org/10.1128/AAC.46.11.3406-3411.2002.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3406-3411
    • Bagge, N.1    Ciofu, O.2    Hentzer, M.3    Campbell, J.I.4    Givskov, M.5    Hoiby, N.6
  • 68
    • 0032570025 scopus 로고    scopus 로고
    • Transcriptional activation of the catechol and chlorocatechol operons: variations on a theme
    • McFall SM, Chugani SA, Chakrabarty AM. 1998. Transcriptional activation of the catechol and chlorocatechol operons: variations on a theme. Gene 223:257-267. http://dx.doi.org/10.1016/S0378-1119(98)00366-7.
    • (1998) Gene , vol.223 , pp. 257-267
    • McFall, S.M.1    Chugani, S.A.2    Chakrabarty, A.M.3
  • 69
    • 0023644752 scopus 로고
    • Purification of the CysB protein from Salmonella typhimurium
    • Miller BE, Kredich NM. 1987. Purification of the CysB protein from Salmonella typhimurium. J. Biol. Chem. 262:6006-6009.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6006-6009
    • Miller, B.E.1    Kredich, N.M.2
  • 70
    • 0344406163 scopus 로고    scopus 로고
    • Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
    • Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, Senda T. 2003. Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J. Mol. Biol. 328:555-566. http://dx.doi.org/10.1016/S0022-2836(03)00312-7.
    • (2003) J. Mol. Biol. , vol.328 , pp. 555-566
    • Muraoka, S.1    Okumura, R.2    Ogawa, N.3    Nonaka, T.4    Miyashita, K.5    Senda, T.6
  • 71
    • 0026495342 scopus 로고
    • Roles of CatR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida
    • Parsek MR, Shinabarger DL, Rothmel RK, Chakrabarty AM. 1992. Roles of CatR and cis,cis-muconate in activation of the catBC operon, which is involved in benzoate degradation in Pseudomonas putida. J. Bacteriol. 174:7798-7806.
    • (1992) J. Bacteriol. , vol.174 , pp. 7798-7806
    • Parsek, M.R.1    Shinabarger, D.L.2    Rothmel, R.K.3    Chakrabarty, A.M.4
  • 72
    • 0025214239 scopus 로고
    • Use of saturation mutagenesis to localize probable functional domains in the NahR protein, a LysR-type transcription activator
    • Schell MA, Brown PH, Raju S. 1990. Use of saturation mutagenesis to localize probable functional domains in the NahR protein, a LysR-type transcription activator. J. Biol. Chem. 265:3844-3850.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3844-3850
    • Schell, M.A.1    Brown, P.H.2    Raju, S.3
  • 73
    • 77954624016 scopus 로고    scopus 로고
    • Crystal structure of the AmpR effector binding domain provides insight into the molecular regulation of inducible Ampc β-lactamase
    • Balcewich MD, Reeve TM, Orlikow EA, Donald LJ, Vocadlo DJ, Mark BL. 2010. Crystal structure of the AmpR effector binding domain provides insight into the molecular regulation of inducible Ampc β-lactamase. J. Mol. Biol. 400:998-1010. http://dx.doi.org/10.1016/j.jmb.2010.05.040.
    • (2010) J. Mol. Biol. , vol.400 , pp. 998-1010
    • Balcewich, M.D.1    Reeve, T.M.2    Orlikow, E.A.3    Donald, L.J.4    Vocadlo, D.J.5    Mark, B.L.6
  • 74
    • 0027447435 scopus 로고
    • Overproduction, solubilization, purification and DNA-binding properties of AmpR from Citrobacter freundii
    • Bishop RE, Weiner JH. 1993. Overproduction, solubilization, purification and DNA-binding properties of AmpR from Citrobacter freundii. Eur. J. Biochem. 213:405-412. http://dx.doi.org/10.1111/j.1432-1033.1993.tb17775.x.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 405-412
    • Bishop, R.E.1    Weiner, J.H.2
  • 75
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132. http://dx.doi.org/10.1016/0022-2836(82)90515-0.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 76
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 77
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method
    • Cserzo M, Wallin E, Simon I, von Heijne G, Elofsson A. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10:673-676. http://dx.doi.org/10.1093/protein/10.6.673.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    von Heijne, G.4    Elofsson, A.5
  • 78
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones DT, Taylor WR, Thornton JM. 1994. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry 33:3038-3049. http://dx.doi.org/10.1021/bi00176a037.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 79
    • 0000207681 scopus 로고
    • A database of membrane spanning protein segments
    • Hofmann K, Stoffel W. 1993. A database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374:166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 83
    • 0024726723 scopus 로고
    • Subcellular localization of the nodD gene product in Rhizobium leguminosarum
    • Schlaman HR, Spaink HP, Okker RJ, Lugtenberg BJ. 1989. Subcellular localization of the nodD gene product in Rhizobium leguminosarum. J. Bacteriol. 171:4686-4693.
    • (1989) J. Bacteriol. , vol.171 , pp. 4686-4693
    • Schlaman, H.R.1    Spaink, H.P.2    Okker, R.J.3    Lugtenberg, B.J.4
  • 84
    • 0028004066 scopus 로고
    • Altered pH and lysine signalling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon
    • Dell CL, Neely MN, Olson ER. 1994. Altered pH and lysine signalling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon. Mol. Microbiol. 14:7-16. http://dx.doi.org/10.1111/j.1365-2958.1994.tb01262.x.
    • (1994) Mol. Microbiol. , vol.14 , pp. 7-16
    • Dell, C.L.1    Neely, M.N.2    Olson, E.R.3
  • 85
    • 78650897914 scopus 로고    scopus 로고
    • Membrane topology and DNAbinding ability of the streptococcal CpsA protein
    • Hanson BR, Lowe BA, Neely MN. 2011. Membrane topology and DNAbinding ability of the streptococcal CpsA protein. J. Bacteriol. 193:411-420. http://dx.doi.org/10.1128/JB.01098-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 411-420
    • Hanson, B.R.1    Lowe, B.A.2    Neely, M.N.3
  • 86
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller VL, Taylor RK, Mekalanos JJ. 1987. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell 48:271-279. http://dx.doi.org/10.1016/0092-8674(87)90430-2.
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 87
    • 84893304286 scopus 로고    scopus 로고
    • Deep sequencing analyses expands the Pseudomonas aeruginosa AmpR regulon to include small RNA-mediated regulation of iron acquisition, heat shock and oxidative stress response
    • Balasubramanian D, Kumari H, Jaric M, Fernandez M, Turner KH, Dove SL, Narasimhan G, Lory S, Mathee K. 2014. Deep sequencing analyses expands the Pseudomonas aeruginosa AmpR regulon to include small RNA-mediated regulation of iron acquisition, heat shock and oxidative stress response. Nucleic Acids Res. 42:979-998. http://dx.doi.org/10.1093/nar/gkt942.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 979-998
    • Balasubramanian, D.1    Kumari, H.2    Jaric, M.3    Fernandez, M.4    Turner, K.H.5    Dove, S.L.6    Narasimhan, G.7    Lory, S.8    Mathee, K.9


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