메뉴 건너뛰기




Volumn 416, Issue 1, 2012, Pages 46-56

An exclusive α/β code directs allostery in TetR-peptide complexes

Author keywords

allostery; anti inducers; bacterial repressor; crystal structures; peptidic effectors

Indexed keywords

SYNTHETIC PEPTIDE; TETRACYCLINE; UREA;

EID: 84856433008     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.12.008     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q., and Karplus M. Allostery and cooperativity revisited Protein Sci. 17 2008 1295 1307
    • (2008) Protein Sci. , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 2
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • DOI 10.1016/S0079-6107(96)00010-7, PII S0079610796000107
    • Jardetzky O. Protein dynamics and conformational transitions in allosteric proteins Prog. Biophys. Mol. Biol. 65 1996 171 219 (Pubitemid 27164026)
    • (1996) Progress in Biophysics and Molecular Biology , vol.65 , Issue.3 , pp. 171-219
    • Jardetzky, O.1
  • 3
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • DOI 10.1016/j.sbi.2003.10.008
    • Kern D., and Zuiderweg E.R. The role of dynamics in allosteric regulation Curr. Opin. Struct. Biol. 13 2003 748 757 (Pubitemid 37522151)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.6 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.P.2
  • 4
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • DOI 10.1002/prot.20232
    • Gunasekaran K., Ma B.Y., and Nussinov R. Is allostery an intrinsic property of all dynamic proteins? Proteins Struct. Funct. Bioinf. 57 2004 433 443 (Pubitemid 39390799)
    • (2004) Proteins: Structure, Function and Genetics , vol.57 , Issue.3 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 5
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms
    • Tsai C.J., Del Sol A., and Nussinov R. Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms Mol. Biosyst. 5 2009 207 216
    • (2009) Mol. Biosyst. , vol.5 , pp. 207-216
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 7
    • 7944232688 scopus 로고    scopus 로고
    • Gene regulation by tetracyclines
    • Berens C., and Hillen W. Gene regulation by tetracyclines Genet. Eng. (NY) 26 2004 255 277
    • (2004) Genet. Eng. (NY) , vol.26 , pp. 255-277
    • Berens, C.1    Hillen, W.2
  • 8
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J., Wyman J., and Changeux J.P. On the nature of allosteric transitions: a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 9
    • 0024295009 scopus 로고
    • Dynamics of repressor-operator recognition: The Tn10-encoded tetracycline resistance control
    • Kleinschmidt C., Tovar K., Hillen W., and Porschke D. Dynamics of repressor-operator recognition: the Tn10-encoded tetracycline resistance control Biochemistry 27 1988 1094 1104
    • (1988) Biochemistry , vol.27 , pp. 1094-1104
    • Kleinschmidt, C.1    Tovar, K.2    Hillen, W.3    Porschke, D.4
  • 10
    • 0029952367 scopus 로고    scopus 로고
    • Tetracycline analogs affecting binding to Tn10-encoded Tet repressor trigger the same mechanism of induction
    • DOI 10.1021/bi952683e
    • Lederer T., Kintrup M., Takahashi M., Sum P.E., Ellestad G.A., and Hillen W. Tetracycline analogs affecting binding to Tn10-encoded Tet repressor trigger the same mechanism of induction Biochemistry 35 1996 7439 7446 (Pubitemid 26189809)
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7439-7446
    • Lederer, T.1    Kintrup, M.2    Takahashi, M.3    Sum, P.-E.4    Ellestad, G.A.5    Hillen, W.6
  • 11
    • 0029593631 scopus 로고
    • Thermodynamic analysis of tetracycline-mediated induction of Tet repressor by a quantitative methylation protection assay
    • DOI 10.1006/abio.1995.0006
    • Lederer T., Takahashi M., and Hillen W. Thermodynamic analysis of tetracycline-mediated induction of Tet repressor by a quantitative methylation protection assay Anal. Biochem. 232 1995 190 196 (Pubitemid 26010258)
    • (1995) Analytical Biochemistry , vol.232 , Issue.2 , pp. 190-196
    • Lederer, T.1    Takahashi, M.2    Hillen, W.3
  • 12
    • 0015240872 scopus 로고
    • Extensions of the allosteric model for haemoglobin
    • Edelstein S.J. Extensions of the allosteric model for haemoglobin Nature 230 1971 224 227
    • (1971) Nature , vol.230 , pp. 224-227
    • Edelstein, S.J.1
  • 13
    • 0022508442 scopus 로고
    • Kinetic and equilibrium characterization of the Tet repressor- tetracycline complex by fluorescence measurements. Evidence for divalent metal ion requirement and energy transfer
    • Takahashi M., Altschmied L., and Hillen W. Kinetic and equilibrium characterization of the Tet repressor-tetracycline complex by fluorescence measurements. Evidence for divalent metal ion requirement and energy transfer J. Mol. Biol. 187 1986 341 348 (Pubitemid 16083776)
    • (1986) Journal of Molecular Biology , vol.187 , Issue.3 , pp. 341-348
    • Takahashi, M.1    Altschmied, L.2    Hillen, W.3
  • 15
    • 0014360315 scopus 로고
    • The interaction of hemoglobin and its subunits with 2,3- diphosphoglycerate
    • Benesch R., Benesch R.E., and Enoki Y. The interaction of hemoglobin and its subunits with 2,3-diphosphoglycerate Proc. Natl Acad. Sci. USA 61 1968 1102 1106
    • (1968) Proc. Natl Acad. Sci. USA , vol.61 , pp. 1102-1106
    • Benesch, R.1    Benesch, R.E.2    Enoki, Y.3
  • 16
    • 41949133232 scopus 로고    scopus 로고
    • Tet repressor induction by tetracycline: A molecular dynamics, continuum electrostatics, and crystallographic study
    • Aleksandrov A., Schuldt L., Hinrichs W., and Simonson T. Tet repressor induction by tetracycline: a molecular dynamics, continuum electrostatics, and crystallographic study J. Mol. Biol. 378 2008 898 912
    • (2008) J. Mol. Biol. , vol.378 , pp. 898-912
    • Aleksandrov, A.1    Schuldt, L.2    Hinrichs, W.3    Simonson, T.4
  • 17
    • 0021658956 scopus 로고
    • Allostery without conformational change. A plausible model
    • Cooper A., and Dryden D.T. Allostery without conformational change. A plausible model Eur. Biophys. J. 11 1984 103 109
    • (1984) Eur. Biophys. J. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.2
  • 18
    • 41149104308 scopus 로고    scopus 로고
    • Allostery: Absence of a change in shape does not imply that allostery is not at play
    • Tsai C.J., del Sol A., and Nussinov R. Allostery: absence of a change in shape does not imply that allostery is not at play J. Mol. Biol. 378 2008 1 11
    • (2008) J. Mol. Biol. , vol.378 , pp. 1-11
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 19
    • 0024239407 scopus 로고
    • Thermal denaturation of engineered Tet repressor proteins and their complexes with tet operator and tetracycline studied by temperature gradient gel electrophoresis
    • DOI 10.1016/0003-2697(88)90566-0
    • Wagenhofer M., Hansen D., and Hillen W. Thermal denaturation of engineered tet repressor proteins and their complexes with tet operator and tetracycline studied by temperature gradient gel electrophoresis Anal. Biochem. 175 1988 422 432 (Pubitemid 19020403)
    • (1988) Analytical Biochemistry , vol.175 , Issue.2 , pp. 422-432
    • Wagenhofer, M.1    Hansen, D.2    Hillen, W.3
  • 20
    • 76049113822 scopus 로고    scopus 로고
    • The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor
    • Reichheld S.E., Yu Z., and Davidson A.R. The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor Proc. Natl Acad. Sci. USA 106 2009 22263 22268
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 22263-22268
    • Reichheld, S.E.1    Yu, Z.2    Davidson, A.R.3
  • 21
    • 84856411134 scopus 로고    scopus 로고
    • Short peptides act as inducers, anti-inducers and corepressors of Tet repressor
    • 10.1016/j.jmb.2011.12.009
    • Goeke D., Kaspar D., Stoeckle C., Grubmüller S., Berens C., and Klotzsche M. Short peptides act as inducers, anti-inducers and corepressors of Tet repressor J. Mol. Biol. 2011 10.1016/j.jmb.2011.12.009
    • (2011) J. Mol. Biol.
    • Goeke, D.1    Kaspar, D.2    Stoeckle, C.3    Grubmüller, S.4    Berens, C.5    Klotzsche, M.6
  • 22
    • 0030055653 scopus 로고    scopus 로고
    • Bi-directional gene switching with the tetracycline repressor and a novel tetracycline antagonist
    • DOI 10.1093/nar/24.15.2900
    • Chrast-Balz J., and Hooft van Huijsduijnen R. Bi-directional gene switching with the tetracycline repressor and a novel tetracycline antagonist Nucleic Acids Res. 24 1996 2900 2904 (Pubitemid 26257155)
    • (1996) Nucleic Acids Research , vol.24 , Issue.15 , pp. 2900-2904
    • Chrast-Balz, J.1    Van Huijsduijnen, R.H.2
  • 23
    • 34047092739 scopus 로고    scopus 로고
    • How an Agonist Peptide Mimics the Antibiotic Tetracycline to Induce Tet-Repressor
    • DOI 10.1016/j.jmb.2007.02.030, PII S0022283607002112
    • Luckner S.R., Klotzsche M., Berens C., Hillen W., and Muller Y.A. How an agonist peptide mimics the antibiotic tetracycline to induce tet-repressor J. Mol. Biol. 368 2007 780 790 (Pubitemid 46527612)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.3 , pp. 780-790
    • Luckner, S.R.1    Klotzsche, M.2    Berens, C.3    Hillen, W.4    Muller, Y.A.5
  • 24
    • 0034087676 scopus 로고    scopus 로고
    • Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system
    • DOI 10.1038/73324
    • Orth P., Schnappinger D., Hillen W., Saenger W., and Hinrichs W. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system Nat. Struct. Biol. 7 2000 215 219 (Pubitemid 30140767)
    • (2000) Nature Structural Biology , vol.7 , Issue.3 , pp. 215-219
    • Orth, P.1    Schnappinger, D.2    Hillen, W.3    Saenger, W.4    Hinrichs, W.5
  • 25
    • 21644478380 scopus 로고    scopus 로고
    • A peptide triggers allostery in Tet repressor by binding to a unique site
    • DOI 10.1074/jbc.M501872200
    • Klotzsche M., Berens C., and Hillen W. A peptide triggers allostery in tet repressor by binding to a unique site J. Biol. Chem. 280 2005 24591 24599 (Pubitemid 40934547)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24591-24599
    • Klotzsche, M.1    Berens, C.2    Hillen, W.3
  • 27
    • 0344874704 scopus 로고    scopus 로고
    • A differential scanning calorimetry study of tetracycline repressor
    • DOI 10.1046/j.1432-1033.2003.03856.x
    • Kedracka-Krok S., and Wasylewski Z. A differential scanning calorimetry study of tetracycline repressor Eur. J. Biochem. 270 2003 4564 4573 (Pubitemid 37452533)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.22 , pp. 4564-4573
    • Kedracka-Krok, S.1    Wasylewski, Z.2
  • 28
  • 29
    • 76049085126 scopus 로고    scopus 로고
    • Regulating transcription regulators via allostery and flexibility
    • Beckett D. Regulating transcription regulators via allostery and flexibility Proc. Natl Acad. Sci. USA 106 2009 22035 22036
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 22035-22036
    • Beckett, D.1
  • 30
    • 48349098865 scopus 로고    scopus 로고
    • A protein functional leap: How a single mutation reverses the function of the transcription regulator TetR
    • Resch M., Striegl H., Henssler E.M., Sevvana M., Egerer-Sieber C., and Schiltz E. A protein functional leap: how a single mutation reverses the function of the transcription regulator TetR Nucleic Acids Res. 36 2008 4390 4401
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4390-4401
    • Resch, M.1    Striegl, H.2    Henssler, E.M.3    Sevvana, M.4    Egerer-Sieber, C.5    Schiltz, E.6
  • 31
    • 77954384737 scopus 로고    scopus 로고
    • A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators
    • Yu Z., Reichheld S.E., Savchenko A., Parkinson J., and Davidson A.R. A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators J. Mol. Biol. 400 2010 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
  • 32
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • DOI 10.1107/S0907444901019291
    • Schneider T.R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules Acta Crystallogr., Sect. D: Biol. Crystallogr. 58 2002 195 208 (Pubitemid 34179189)
    • (2002) Acta Crystallographica Section D: Biological Crystallography , vol.58 , Issue.2 , pp. 195-208
    • Schneider, T.R.1
  • 33
    • 70449825814 scopus 로고    scopus 로고
    • Induction of the tetracycline repressor: Characterization by molecular-dynamics simulations
    • Haberl F., Lanig H., and Clark T. Induction of the tetracycline repressor: characterization by molecular-dynamics simulations Proteins 77 2009 857 866
    • (2009) Proteins , vol.77 , pp. 857-866
    • Haberl, F.1    Lanig, H.2    Clark, T.3
  • 34
    • 26944466128 scopus 로고    scopus 로고
    • Regulation of AmtR-controlled gene expression in Corynebacterium glutamicum: Mechanism and characterization of the AmtR regulon
    • DOI 10.1111/j.1365-2958.2005.04855.x
    • Beckers G., Strosser J., Hildebrandt U., Kalinowski J., Farwick M., Kramer R., and Burkovski A. Regulation of AmtR-controlled gene expression in Corynebacterium glutamicum: mechanism and characterization of the AmtR regulon Mol. Microbiol. 58 2005 580 595 (Pubitemid 41476170)
    • (2005) Molecular Microbiology , vol.58 , Issue.2 , pp. 580-595
    • Beckers, G.1    Strosser, J.2    Hildebrandt, U.3    Kalinowski, J.4    Farwick, M.5    Kramer, R.6    Burkovski, A.7
  • 35
    • 6344275007 scopus 로고    scopus 로고
    • Modulation of AraC family member activity by protein ligands
    • DOI 10.1111/j.1365-2958.2004.04306.x
    • Plano G.V. Modulation of AraC family member activity by protein ligands Mol. Microbiol. 54 2004 287 290 (Pubitemid 39388274)
    • (2004) Molecular Microbiology , vol.54 , Issue.2 , pp. 287-290
    • Plano, G.V.1
  • 36
    • 4544356004 scopus 로고    scopus 로고
    • Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P
    • DOI 10.1016/j.cell.2004.08.027, PII S0092867404007925
    • Schumacher M.A., Allen G.S., Diel M., Seidel G., Hillen W., and Brennan R.G. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P Cell 118 2004 731 741 (Pubitemid 39221732)
    • (2004) Cell , vol.118 , Issue.6 , pp. 731-741
    • Schumacher, M.A.1    Allen, G.S.2    Diel, M.3    Seidel, G.4    Hillen, W.5    Brennan, R.G.6
  • 38
    • 0019586165 scopus 로고
    • Mechanism of action of the lexA gene product
    • Brent R., and Ptashne M. Mechanism of action of the lexA gene product Proc. Natl Acad. Sci. USA 78 1981 4204 4208
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4204-4208
    • Brent, R.1    Ptashne, M.2
  • 41
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 2007 32 41
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 44
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • DOI 10.1038/8263
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6 1999 458 463 (Pubitemid 29218016)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 47
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors Acta Crystallogr., Sect. A 32 1976 922 923
    • (1976) Acta Crystallogr., Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.