메뉴 건너뛰기




Volumn 194, Issue 17, 2012, Pages 4630-4641

Transcriptional repression mediated by a TetR family protein, PfmR, from Thermus thermophilus HB8

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PFMR PROTEIN; PHENYLACETIC ACID; QACR PROTEIN; UNCLASSIFIED DRUG;

EID: 84866314912     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00668-12     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 79958166755 scopus 로고    scopus 로고
    • TetR family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation
    • Agari Y, Agari K, Sakamoto K, Kuramitsu S, Shinkai A. 2011. TetR family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation. Microbiology 157:1589-1601.
    • (2011) Microbiology , vol.157 , pp. 1589-1601
    • Agari, Y.1    Agari, K.2    Sakamoto, K.3    Kuramitsu, S.4    Shinkai, A.5
  • 2
    • 51649108915 scopus 로고    scopus 로고
    • Global gene expression mediated by Thermus thermophilus SdrP, a CRP/ FNR family transcriptional regulator
    • Agari Y, Kashihara A, Yokoyama S, Kuramitsu S, Shinkai A. 2008. Global gene expression mediated by Thermus thermophilus SdrP, a CRP/ FNR family transcriptional regulator. Mol. Microbiol. 70:60-75.
    • (2008) Mol. Microbiol. , vol.70 , pp. 60-75
    • Agari, Y.1    Kashihara, A.2    Yokoyama, S.3    Kuramitsu, S.4    Shinkai, A.5
  • 4
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. 1998. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54:905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 8
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P, Robert X, Courcelle E. 2003. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31:3320-3323.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 9
    • 0032541162 scopus 로고    scopus 로고
    • QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA
    • Grkovic S, Brown MH, Roberts NJ, Paulsen IT, Skurray RA. 1998. QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA. J. Biol. Chem. 273:18665-18673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18665-18673
    • Grkovic, S.1    Brown, M.H.2    Roberts, N.J.3    Paulsen, I.T.4    Skurray, R.A.5
  • 10
    • 0035205399 scopus 로고    scopus 로고
    • The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers
    • Grkovic S, Brown MH, Schumacher MA, Brennan RG, Skurray RA. 2001. The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers. J. Bacteriol. 183:7102-7109.
    • (2001) J. Bacteriol. , vol.183 , pp. 7102-7109
    • Grkovic, S.1    Brown, M.H.2    Schumacher, M.A.3    Brennan, R.G.4    Skurray, R.A.5
  • 11
    • 0035850879 scopus 로고    scopus 로고
    • Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin-resistant marker
    • Hashimoto Y, Yano T, Kuramitsu S, Kagamiyama H. 2001. Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin-resistant marker. FEBS Lett. 506:231-234.
    • (2001) FEBS Lett. , vol.506 , pp. 231-234
    • Hashimoto, Y.1    Yano, T.2    Kuramitsu, S.3    Kagamiyama, H.4
  • 12
    • 0028244325 scopus 로고
    • Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
    • Hinrichs W, et al. 1994. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science 264:418-420.
    • (1994) Science , vol.264 , pp. 418-420
    • Hinrichs, W.1
  • 13
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 15
    • 0025366034 scopus 로고
    • Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity
    • Kuramitsu S, Hiromi K, Hayashi H, Morino Y, Kagamiyama H. 1990. Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry 29:5469-5476.
    • (1990) Biochemistry , vol.29 , pp. 5469-5476
    • Kuramitsu, S.1    Hiromi, K.2    Hayashi, H.3    Morino, Y.4    Kagamiyama, H.5
  • 16
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2
    • Larkin MA, et al. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948.
    • (2007) 0. Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 17
    • 82255194409 scopus 로고    scopus 로고
    • The crystal structure of the TetR family transcriptional repressor SimR bound to DNA and the role of a flexible N-terminal extension in minor groove binding
    • Le TB, Schumacher MA, Lawson DM, Brennan RG, Buttner MJ. 2011. The crystal structure of the TetR family transcriptional repressor SimR bound to DNA and the role of a flexible N-terminal extension in minor groove binding. Nucleic Acids Res. 39:9433-9447.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9433-9447
    • Le, T.B.1    Schumacher, M.A.2    Lawson, D.M.3    Brennan, R.G.4    Buttner, M.J.5
  • 18
    • 79953239922 scopus 로고    scopus 로고
    • Structures of the TetR-like simocyclinone efflux pump repressor, SimR, and the mechanism of ligand-mediated derepression
    • Le TB, et al. 2011. Structures of the TetR-like simocyclinone efflux pump repressor, SimR, and the mechanism of ligand-mediated derepression. J. Mol. Biol. 408:40-56.
    • (2011) J. Mol. Biol. , vol.408 , pp. 40-56
    • Le, T.B.1
  • 19
    • 0022273106 scopus 로고
    • 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type
    • LeMaster DM, Richards FM. 1985. 1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type. Biochemistry 24:7263-7268.
    • (1985) Biochemistry , vol.24 , pp. 7263-7268
    • Lemaster, D.M.1    Richards, F.M.2
  • 20
    • 0035057115 scopus 로고    scopus 로고
    • The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications
    • Luengo JM, Garcia JL, Olivera ER. 2001. The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications. Mol. Microbiol. 39:1434-1442.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1434-1442
    • Luengo, J.M.1    Garcia, J.L.2    Olivera, E.R.3
  • 21
    • 0036087630 scopus 로고    scopus 로고
    • CDD: a database of conserved domain alignments with links to domain three-dimensional structure
    • Marchler-Bauer A, et al. 2002. CDD: a database of conserved domain alignments with links to domain three-dimensional structure. Nucleic Acids Res. 30:281-283.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 281-283
    • Marchler-Bauer, A.1
  • 22
    • 77950656400 scopus 로고    scopus 로고
    • A novel role of malonyl-ACP in lipid homeostasis
    • Martinez MA, et al. 2010. A novel role of malonyl-ACP in lipid homeostasis. Biochemistry 49:3161-3167.
    • (2010) Biochemistry , vol.49 , pp. 3161-3167
    • Martinez, M.A.1
  • 23
    • 33646596266 scopus 로고    scopus 로고
    • Genome-wide survey of transcription factors in prokaryotes reveals many bacteria-specific families not found in archaea
    • Minezaki Y, Homma K, Nishikawa K. 2005. Genome-wide survey of transcription factors in prokaryotes reveals many bacteria-specific families not found in archaea. DNA Res. 12:269-280.
    • (2005) DNA Res. , vol.12 , pp. 269-280
    • Minezaki, Y.1    Homma, K.2    Nishikawa, K.3
  • 24
    • 84857914339 scopus 로고    scopus 로고
    • The third plasmid pVV8 from Thermus thermophilus HB8: isolation, characterization, and sequence determination
    • Ohtani N, Tomita M, Itaya M. 2012. The third plasmid pVV8 from Thermus thermophilus HB8: isolation, characterization, and sequence determination. Extremophiles 16:237-244.
    • (2012) Extremophiles , vol.16 , pp. 237-244
    • Ohtani, N.1    Tomita, M.2    Itaya, M.3
  • 25
    • 0032486128 scopus 로고    scopus 로고
    • Conformational changes of the Tet repressor induced by tetracycline trapping
    • Orth P, et al. 1998. Conformational changes of the Tet repressor induced by tetracycline trapping. J. Mol. Biol. 279:439-447.
    • (1998) J. Mol. Biol. , vol.279 , pp. 439-447
    • Orth, P.1
  • 26
    • 0034087676 scopus 로고    scopus 로고
    • Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system.
    • Orth P, Schnappinger D, Hillen W, Saenger W, Hinrichs W. 2000. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system. Nat. Struct. Biol. 7:215-219.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 215-219
    • Orth, P.1    Schnappinger, D.2    Hillen, W.3    Saenger, W.4    Hinrichs, W.5
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 20544432535 scopus 로고    scopus 로고
    • The TetR family of transcriptional repressors
    • Ramos JL, et al. 2005. The TetR family of transcriptional repressors. Microbiol. Mol. Biol. Rev. 69:326-356.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 326-356
    • Ramos, J.L.1
  • 31
    • 76049113822 scopus 로고    scopus 로고
    • The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor
    • Reichheld SE, Yu Z, Davidson AR. 2009. The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor. Proc. Natl. Acad. Sci. U. S. A. 106:22263-22268.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22263-22268
    • Reichheld, S.E.1    Yu, Z.2    Davidson, A.R.3
  • 32
    • 34548219522 scopus 로고    scopus 로고
    • Comparative genomic reconstruction of transcriptional regulatory networks in bacteria
    • Rodionov DA. 2007. Comparative genomic reconstruction of transcriptional regulatory networks in bacteria. Chem. Rev. 107:3467-3497.
    • (2007) Chem. Rev. , vol.107 , pp. 3467-3497
    • Rodionov, D.A.1
  • 33
    • 80052322974 scopus 로고    scopus 로고
    • Phenylacetyl coenzyme A is an effector molecule of the TetR family transcriptional repressor PaaR from Thermus thermophilus HB8
    • Sakamoto K, Agari Y, Kuramitsu S, Shinkai A. 2011. Phenylacetyl coenzyme A is an effector molecule of the TetR family transcriptional repressor PaaR from Thermus thermophilus HB8. J. Bacteriol. 193:4388-4395.
    • (2011) J. Bacteriol. , vol.193 , pp. 4388-4395
    • Sakamoto, K.1    Agari, Y.2    Kuramitsu, S.3    Shinkai, A.4
  • 34
    • 0036500260 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR
    • Schumacher MA, et al. 2002. Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR. EMBO J. 21: 1210-1218.
    • (2002) EMBO J. , vol.21 , pp. 1210-1218
    • Schumacher, M.A.1
  • 35
    • 0035824388 scopus 로고    scopus 로고
    • Structural mechanisms of QacR induction and multidrug recognition
    • Schumacher MA, et al. 2001. Structural mechanisms of QacR induction and multidrug recognition. Science 294:2158-2163.
    • (2001) Science , vol.294 , pp. 2158-2163
    • Schumacher, M.A.1
  • 36
    • 34248359835 scopus 로고    scopus 로고
    • Transcription activation mediated by a cyclic AMP receptor protein from Thermus thermophilus HB8
    • Shinkai A, et al. 2007. Transcription activation mediated by a cyclic AMP receptor protein from Thermus thermophilus HB8. J. Bacteriol. 189:3891-3901.
    • (2007) J. Bacteriol. , vol.189 , pp. 3891-3901
    • Shinkai, A.1
  • 39
    • 77956292377 scopus 로고    scopus 로고
    • Bacterial phenylalanine and phenylacetate catabolic pathway revealed
    • Teufel R, et al. 2010. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. U. S. A. 107:14390-14395.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14390-14395
    • Teufel, R.1
  • 40
    • 33747670167 scopus 로고    scopus 로고
    • RIKEN structural genomics beamlines at the SPring-8; high throughput protein crystallography with automated beamline operation
    • Ueno G, et al. 2006. RIKEN structural genomics beamlines at the SPring-8; high throughput protein crystallography with automated beamline operation. J. Struct. Funct. Genomics 7:15-22.
    • (2006) J. Struct. Funct. Genomics , vol.7 , pp. 15-22
    • Ueno, G.1
  • 41
    • 39149132467 scopus 로고    scopus 로고
    • Crystal structures of the Streptomyces coelicolor TetR-like protein ActR alone and in complex with actinorhodin or the actinorhodin biosynthetic precursor (S)-DNPA
    • Willems AR, et al. 2008. Crystal structures of the Streptomyces coelicolor TetR-like protein ActR alone and in complex with actinorhodin or the actinorhodin biosynthetic precursor (S)-DNPA. J. Mol. Biol. 376:1377-1387.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1377-1387
    • Willems, A.R.1
  • 42
    • 77954384737 scopus 로고    scopus 로고
    • A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators
    • Yu Z, Reichheld SE, Savchenko A, Parkinson J, Davidson AR. 2010. A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators. J. Mol. Biol. 400:847-864.
    • (2010) J. Mol. Biol. , vol.400 , pp. 847-864
    • Yu, Z.1    Reichheld, S.E.2    Savchenko, A.3    Parkinson, J.4    Davidson, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.