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Volumn 105, Issue 31, 2008, Pages 10709-10714

Light-activated DNA binding in a designed allosteric protein

Author keywords

Allostery; Alpha helix; LOV domain; Protein design; trp repressor

Indexed keywords

CELL MEMBRANE PROTEIN; NUCLEASE; PHOTOTROPIN 1; TRYPTOPHAN;

EID: 49449118042     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0709610105     Document Type: Article
Times cited : (254)

References (46)
  • 1
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya RP, Remenyi A, Yeh BJ, Lim WA (2006) Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits. Annu Rev Biochem 75:655-680.
    • (2006) Annu Rev Biochem , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 2
    • 14844321287 scopus 로고    scopus 로고
    • Synthetic modular systems - Reverse engineering of signal transduction
    • Pawson T, Linding R (2005) Synthetic modular systems - Reverse engineering of signal transduction. FEBS Lett 579:1808-1814.
    • (2005) FEBS Lett , vol.579 , pp. 1808-1814
    • Pawson, T.1    Linding, R.2
  • 3
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300:445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 5
    • 23944444109 scopus 로고    scopus 로고
    • Engineering allosteric protein switches by domain insertion
    • Ostermeier M (2005) Engineering allosteric protein switches by domain insertion. Protein Eng Des Sel 18:359-364.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 359-364
    • Ostermeier, M.1
  • 6
    • 0028588070 scopus 로고
    • Domain insertion
    • Russell RB (1994) Domain insertion. Protein Eng 7:1407-1410.
    • (1994) Protein Eng , vol.7 , pp. 1407-1410
    • Russell, R.B.1
  • 7
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird GS, Zacharias DA, Tsien RY (1999) Circular permutation and receptor insertion within green fluorescent proteins. Proc Natl Acad Sci USA 96:11241-11246.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 8
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas G, Mansell TJ, Kim JR, Ostermeier M (2005) Directed evolution of protein switches and their application to the creation of ligand-binding proteins. Proc Natl Acad Sci USA 102:11224-11229.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11224-11229
    • Guntas, G.1    Mansell, T.J.2    Kim, J.R.3    Ostermeier, M.4
  • 10
    • 35448990907 scopus 로고    scopus 로고
    • A modular and extensible RNA-based gene-regulatory platform for engineering cellular function
    • Win MN, Smolke CD (2007) A modular and extensible RNA-based gene-regulatory platform for engineering cellular function. Proc Natl Acad Sci USA 104:14283-14288.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14283-14288
    • Win, M.N.1    Smolke, C.D.2
  • 11
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran K, Ma B, Nussinov R (2004) Is allostery an intrinsic property of all dynamic proteins? Proteins 57:433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 12
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire E (1999) The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc Natl Acad Sci USA 96:10118-10122.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10118-10122
    • Freire, E.1
  • 13
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser VJ, Thompson EB (2007) Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci USA 104:8311-8315.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 14
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman BF, Lipson D, Wemmer DE, Kern D (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291:2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 15
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 16
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber JE, Yeh BJ, Chak K, Lim WA (2003) Reprogramming control of an allosteric signaling switch through modular recombination. Science 301:1904-1908.
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 17
    • 34247465989 scopus 로고    scopus 로고
    • Engineering modular protein interaction switches by sequence overlap
    • Sallee NA, Yeh BJ, Lim WA (2007) Engineering modular protein interaction switches by sequence overlap. J Am Chem Soc 129:4606-4611.
    • (2007) J Am Chem Soc , vol.129 , pp. 4606-4611
    • Sallee, N.A.1    Yeh, B.J.2    Lim, W.A.3
  • 18
    • 0346500466 scopus 로고    scopus 로고
    • Creation of an allosteric enzyme by domain insertion
    • Guntas G, Ostermeier M (2004) Creation of an allosteric enzyme by domain insertion. J Mol Biol 336:263-273.
    • (2004) J Mol Biol , vol.336 , pp. 263-273
    • Guntas, G.1    Ostermeier, M.2
  • 19
    • 24644523298 scopus 로고    scopus 로고
    • Design and folding of a multidomain protein
    • Zhou Z, Feng H, Zhou H, Zhou Y, Bai Y (2005) Design and folding of a multidomain protein. Biochemistry 44:12107-12112.
    • (2005) Biochemistry , vol.44 , pp. 12107-12112
    • Zhou, Z.1    Feng, H.2    Zhou, H.3    Zhou, Y.4    Bai, Y.5
  • 20
    • 22244458915 scopus 로고    scopus 로고
    • Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library
    • Jha AK, et al. (2005) Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library. Biochemistry 44:9691-9702.
    • (2005) Biochemistry , vol.44 , pp. 9691-9702
    • Jha, A.K.1
  • 21
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • Luque I, Freire E (2000) Structural stability of binding sites: Consequences for binding affinity and allosteric effects. Proteins Suppl 4:63-71.
    • (2000) Proteins Suppl , vol.4 , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 22
    • 15444362906 scopus 로고    scopus 로고
    • Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins
    • Whitten ST, Garcia-Moreno EB, Hilser VJ (2005) Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. Proc Natl Acad Sci USA 102:4282-4287.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4282-4287
    • Whitten, S.T.1    Garcia-Moreno, E.B.2    Hilser, V.J.3
  • 23
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala E, et al. (1997) Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain. Science 278:2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1
  • 24
    • 33947412138 scopus 로고    scopus 로고
    • Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: Signaling, dimerization, and mechanism
    • Key J, Hefti M, Purcell EB, Moffat K (2007) Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: Signaling, dimerization, and mechanism. Biochemistry 46:3614-3623.
    • (2007) Biochemistry , vol.46 , pp. 3614-3623
    • Key, J.1    Hefti, M.2    Purcell, E.B.3    Moffat, K.4
  • 25
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • Crosson S, Rajagopal S, Moffat K (2003) The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains. Biochemistry 42:2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 26
    • 34249080375 scopus 로고    scopus 로고
    • Conformational switching in the fungal light sensor Vivid
    • Zoltowski BD, et al. (2007) Conformational switching in the fungal light sensor Vivid. Science 316:1054-1057.
    • (2007) Science , vol.316 , pp. 1054-1057
    • Zoltowski, B.D.1
  • 27
    • 0035965307 scopus 로고    scopus 로고
    • The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin
    • Swartz TE, et al. (2001) The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin. J Biol Chem 276:36493-36500.
    • (2001) J Biol Chem , vol.276 , pp. 36493-36500
    • Swartz, T.E.1
  • 28
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity
    • Harper SM, Christie JM, Gardner KH (2004) Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity. Biochemistry 43:16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 29
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper SM, Neil LC, Gardner KH (2003) Structural basis of a phototropin light switch. Science 301:1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 30
    • 0011023559 scopus 로고
    • Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor
    • Gunsalus RP, Yanofsky C (1980) Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor. Proc Natl Acad Sci USA 77:7117-7121.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7117-7121
    • Gunsalus, R.P.1    Yanofsky, C.2
  • 31
    • 0029131681 scopus 로고
    • Engineering proteins without primary sequence tryptophan residues: Mutant trp repressors with aliphatic substitutions for tryptophan side chains
    • Chapman D, Hochstrasser R, Millar D, Youderian P (1995) Engineering proteins without primary sequence tryptophan residues: Mutant trp repressors with aliphatic substitutions for tryptophan side chains. Gene 163:1-11.
    • (1995) Gene , vol.163 , pp. 1-11
    • Chapman, D.1    Hochstrasser, R.2    Millar, D.3    Youderian, P.4
  • 32
    • 0033534367 scopus 로고    scopus 로고
    • Long-range effects on dynamics in a temperature-sensitive mutant of trp repressor
    • Jin L, Fukayama JW, Pelczer I, Carey J (1999) Long-range effects on dynamics in a temperature-sensitive mutant of trp repressor. J Mol Biol 285:361-378.
    • (1999) J Mol Biol , vol.285 , pp. 361-378
    • Jin, L.1    Fukayama, J.W.2    Pelczer, I.3    Carey, J.4
  • 33
    • 0031596571 scopus 로고    scopus 로고
    • Mutational analysis of the NH2-terminal arms of the trp repressor indicates a multifunctional domain
    • Mackintosh SG, McDermott PF, Hurlburt BK (1998) Mutational analysis of the NH2-terminal arms of the trp repressor indicates a multifunctional domain. Mol Microbiol 27:1119-1127.
    • (1998) Mol Microbiol , vol.27 , pp. 1119-1127
    • Mackintosh, S.G.1    McDermott, P.F.2    Hurlburt, B.K.3
  • 34
    • 0030598345 scopus 로고    scopus 로고
    • Characterization of charge change super-repressor mutants of trp repressor: Effects on oligomerization conformation, ligation and stability
    • Reedstrom RJ, et al. (1996) Characterization of charge change super-repressor mutants of trp repressor: Effects on oligomerization conformation, ligation and stability. J Mol Biol 264:32-45.
    • (1996) J Mol Biol , vol.264 , pp. 32-45
    • Reedstrom, R.J.1
  • 35
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half-site complex
    • Lawson CL, Carey J (1993) Tandem binding in crystals of a trp repressor/operator half-site complex. Nature 366:178-182.
    • (1993) Nature , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 37
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1
    • Corchnoy SB, et al. (2003) Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1. J Biol Chem 278:724-731.
    • (2003) J Biol Chem , vol.278 , pp. 724-731
    • Corchnoy, S.B.1
  • 38
    • 0030792524 scopus 로고    scopus 로고
    • Construction and characterization of monomeric tryptophan repressor: A model for an early intermediate in the folding of a dimeric protein
    • Shao X, Hensley P, Matthews CR (1997) Construction and characterization of monomeric tryptophan repressor: A model for an early intermediate in the folding of a dimeric protein. Biochemistry 36:9941-9949.
    • (1997) Biochemistry , vol.36 , pp. 9941-9949
    • Shao, X.1    Hensley, P.2    Matthews, C.R.3
  • 39
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 25:495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 40
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan P, Henderson SJ, Joachimiak A (1996) Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure (London) 4:79-88.
    • (1996) Structure (London) , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 41
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 42
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
    • Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ (1999) Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 398:84-90.
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 43
    • 0036427580 scopus 로고    scopus 로고
    • The molecular basis of sensing and responding to light in microorganisms
    • Hellingwerf KJ (2002) The molecular basis of sensing and responding to light in microorganisms. Ant V Leeuwenhoek 81:51-59.
    • (2002) Ant V Leeuwenhoek , vol.81 , pp. 51-59
    • Hellingwerf, K.J.1
  • 44
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 45
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 36:860-864.
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 46
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • Halavaty AS, Moffat K (2007) N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry 46:14001-14009.
    • (2007) Biochemistry , vol.46 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2


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