메뉴 건너뛰기




Volumn 16, Issue 24, 1997, Pages 7532-7541

Solution structure of the mu end DNA-binding Iβ subdomain of phage Mu transposase: Modular DNA recognition by two tethered domains

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; TRANSPOSASE;

EID: 0031464544     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.24.7532     Document Type: Article
Times cited : (42)

References (63)
  • 2
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker, T.A. and Luo, L. (1994) Identification of residues in the Mu transposase essential for catalysis. Proc. Natl Acad. Sci. USA, 91, 6654-6658.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 3
    • 0025794342 scopus 로고
    • MuB protein allosterically activates strand transfer by the transposase of phage Mu
    • Baker, T.A., Mizuuchi, M. and Mizuuchi, K. (1991) MuB protein allosterically activates strand transfer by the transposase of phage Mu. Cell, 65, 1003-1013.
    • (1991) Cell , vol.65 , pp. 1003-1013
    • Baker, T.A.1    Mizuuchi, M.2    Mizuuchi, K.3
  • 4
    • 0027203762 scopus 로고
    • Division of labor among monomers in the Mu transposase tetramer
    • Baker, T.A., Mizuuchi, M., Savilahti, H. and Mizuuchi, K. (1993) Division of labor among monomers in the Mu transposase tetramer. Cell, 74, 723-733.
    • (1993) Cell , vol.74 , pp. 723-733
    • Baker, T.A.1    Mizuuchi, M.2    Savilahti, H.3    Mizuuchi, K.4
  • 5
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A. and Grzesiek, S. (1993) Methodological advances in protein NMR. Acc. Chem. Res., 26, 131-138.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 7
    • 0004224917 scopus 로고
    • American Society of Microbiology, Washington, DC
    • Berg, D.E. and Howe, M.M., eds (1989) Mobile DNA. American Society of Microbiology, Washington, DC.
    • (1989) Mobile DNA
    • Berg, D.E.1    Howe, M.M.2
  • 11
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three-and four dimensional heteronuclear NMR spectroscopy
    • Clore, G.M. and Gronenborn, A.M. (1991) Structures of larger proteins in solution: three-and four dimensional heteronuclear NMR spectroscopy. Science, 252, 1390-1399.
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 0028674451 scopus 로고
    • Multidimensional heteronuclcar magnetic resonance of proteins
    • Clore, G.M. and Gronenborn, A.M. (1994) Multidimensional heteronuclcar magnetic resonance of proteins. Methods Enzymol., 239, 349-363.
    • (1994) Methods Enzymol. , vol.239 , pp. 349-363
    • Clore, G.M.1    Gronenborn, A.M.2
  • 13
    • 0028774530 scopus 로고
    • A novel class of winged helix-turn-helix protein: The DNA-binding domain of Mu transposase
    • Clubb, R.T., Omichinski, J.G., Savilahti, H., Mizuuchi, K., Gronenborn, A.M. and Clore, G.M. (1994) A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase. Structure, 2, 1041-1048.
    • (1994) Structure , vol.2 , pp. 1041-1048
    • Clubb, R.T.1    Omichinski, J.G.2    Savilahti, H.3    Mizuuchi, K.4    Gronenborn, A.M.5    Clore, G.M.6
  • 15
    • 0031576325 scopus 로고    scopus 로고
    • Solution structure of the Iγ subdomain of the Mu end DNA binding domain of phage Mu transposase
    • Clubb, R.T., Schumacher, S., Mizuuchi, K., Gronenborn, A.M. and Clore, G.M. (1997) Solution structure of the Iγ subdomain of the Mu end DNA binding domain of phage Mu transposase. J. Mol. Biol., 273, 19-25.
    • (1997) J. Mol. Biol. , vol.273 , pp. 19-25
    • Clubb, R.T.1    Schumacher, S.2    Mizuuchi, K.3    Gronenborn, A.M.4    Clore, G.M.5
  • 16
    • 0021931495 scopus 로고
    • Mechanism of transposition of bacteriophage Mu: Structure of a transposition intermediate
    • Craigie, R. and Mizuuchi, K. (1985) Mechanism of transposition of bacteriophage Mu: structure of a transposition intermediate. Cell, 41, 867-876.
    • (1985) Cell , vol.41 , pp. 867-876
    • Craigie, R.1    Mizuuchi, K.2
  • 17
    • 0023646797 scopus 로고
    • Transposition of Mu DNA: Joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu
    • Craigie, R. and Mizuuchi, K. (1987) Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu. Cell, 51, 493-501.
    • (1987) Cell , vol.51 , pp. 493-501
    • Craigie, R.1    Mizuuchi, K.2
  • 18
    • 0021676867 scopus 로고
    • Site-specific recognition of the bacteriophage Mu ends by the MuA protein
    • Craigie, R., Mizuuchi, M. and Mizuuchi, K. (1984) Site-specific recognition of the bacteriophage Mu ends by the MuA protein. Cell. 39, 387-394.
    • (1984) Cell. , vol.39 , pp. 387-394
    • Craigie, R.1    Mizuuchi, M.2    Mizuuchi, K.3
  • 19
    • 0029400480 scopus 로고
    • NMR Pipe: A multidimensional spectral processing system based on UNIX PIPES
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMR Pipe: a multidimensional spectral processing system based on UNIX PIPES. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 20
    • 0027326864 scopus 로고
    • (+)-CC-1065 as a structural probe of Mu transposase-induced bending of DNA: Overcoming limitations of hydroxyl-radical footprinting
    • Ding, A., Harshey, R.M. and Hurley, L. H. (1993) (+)-CC-1065 as a structural probe of Mu transposase-induced bending of DNA: overcoming limitations of hydroxyl-radical footprinting. Nucleic Acids Res., 21, 4281-1287.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4281-11287
    • Ding, A.1    Harshey, R.M.2    Hurley, L.H.3
  • 21
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F., Hickman, A.B., Jenkins, T.M., Engelman, A., Craigie, R. and Davies, D.R. (1994) Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science, 266, 1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 22
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in two-, three- And four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M. (1991) A common-sense approach to peak picking in two-, three-and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Resonance, 95, 214-222.
    • (1991) J. Magn. Resonance , vol.95 , pp. 214-222
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 24
    • 0029609126 scopus 로고
    • DNA transposition: From a black box to a color monitor
    • Grindley, N.D.F. and Leschziner, A.E. (1995) DNA transposition: from a black box to a color monitor. Cell, 83, 1063-1066.
    • (1995) Cell , vol.83 , pp. 1063-1066
    • Grindley, N.D.F.1    Leschziner, A.E.2
  • 26
    • 0030764469 scopus 로고    scopus 로고
    • 13C J couplings measured by three-dimensional heteronuclear NMR: How planar is the peptide bond
    • 13C J couplings measured by three-dimensional heteronuclear NMR: how planar is the peptide bond. J. Am. Chem. Soc., 27, 6360-6368.
    • (1997) J. Am. Chem. Soc. , vol.27 , pp. 6360-6368
    • Hu, J.-S.1    Bax, A.2
  • 27
    • 0031111521 scopus 로고    scopus 로고
    • NCγ couplings in isotopically enriched proteins
    • NCγ couplings in isotopically enriched proteins. J. Biomol. NMR, 9, 323-328.
    • (1997) J. Biomol. NMR , vol.9 , pp. 323-328
    • Hu, J.-S.1    Bax, A.2
  • 29
    • 0028883476 scopus 로고
    • Mutational analysis of the att DNA-binding domain of phage Mu transposase
    • Kim, K. and Harshey, R.M. (1995) Mutational analysis of the att DNA-binding domain of phage Mu transposase. Nucleic Acids Res., 23, 3937-3943.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3937-3943
    • Kim, K.1    Harshey, R.M.2
  • 30
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Konradi, R., Billeter, M. and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 52-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 52-55
    • Konradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 31
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Echerichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis, R., Welty, D.J. and Nakai, H. (1996) ClpX protein of Echerichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J., 15, 935-944.
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 32
    • 0025876672 scopus 로고
    • DNA-protein complexes during attachment-site synapsis in Mu DNA transposition
    • Kuo, C.-F., Zou, A., Jayaram, M., Getzoff, E. and Harshey, R.M. (1991) DNA-protein complexes during attachment-site synapsis in Mu DNA transposition. EMBO J., 10, 1585-1591.
    • (1991) EMBO J. , vol.10 , pp. 1585-1591
    • Kuo, C.-F.1    Zou, A.2    Jayaram, M.3    Getzoff, E.4    Harshey, R.M.5
  • 34
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • Kuszewski, J., Gronenborn, A.M. and Clore, G.M. (1996) Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci., 5, 1067-1080.
    • (1996) Protein Sci. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 35
    • 0031083293 scopus 로고    scopus 로고
    • Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
    • Kuszewski, J., Gronenborn, A.M. and Clore, G.M. (1997) Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J. Magn. Resonance, 125, 171-177.
    • (1997) J. Magn. Resonance , vol.125 , pp. 171-177
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 36
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0025860233 scopus 로고
    • Two mutations of phage Mu transposase that affect strand transfer or interactions with B protein lie in distinct polypeptide domains
    • Leung, P.C. and Harshey, R.M. (1991) Two mutations of phage Mu transposase that affect strand transfer or interactions with B protein lie in distinct polypeptide domains. J. Mol. Biol., 219, 189-199.
    • (1991) J. Mol. Biol. , vol.219 , pp. 189-199
    • Leung, P.C.1    Harshey, R.M.2
  • 39
    • 0024602375 scopus 로고
    • Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer
    • Leung, P.C., Treplow, D.B. and Harshey, R.M. (1989) Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer. Nature, 338, 656-658.
    • (1989) Nature , vol.338 , pp. 656-658
    • Leung, P.C.1    Treplow, D.B.2    Harshey, R.M.3
  • 40
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L. and Baker, T.A. (1995) Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev., 9, 2399-2408.
    • (1995) Genes Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 42
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA
    • Li, T., Stark, M.R., Johnson, A.D. and Wolberger, C. (1995) Crystal structure of the MATa1/MATα2 homeodomain heterodimer bound to DNA. Science, 270, 262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 43
    • 0026353467 scopus 로고
    • Analysis of DNA-protein interactions by affinity coelectrophoresis
    • Lim, W.A., Sauer, R.T. and Lander, A.D. (1991) Analysis of DNA-protein interactions by affinity coelectrophoresis. Methods Enzymol., 208, 196-210.
    • (1991) Methods Enzymol. , vol.208 , pp. 196-210
    • Lim, W.A.1    Sauer, R.T.2    Lander, A.D.3
  • 44
    • 0026637325 scopus 로고
    • Transpositional recombination: Mechanistic insights from studies of Mu and other elements
    • Mizuuchi, K. (1992) Transpositional recombination: mechanistic insights from studies of Mu and other elements. Annu. Rev. Biochem., 61, 1011-1051.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1011-1051
    • Mizuuchi, K.1
  • 45
    • 0024322147 scopus 로고
    • Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: Implications for regulation
    • Mizuuchi, M. and Mizuuchi, K. (1989) Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: implications for regulation. Cell, 58, 399-408.
    • (1989) Cell , vol.58 , pp. 399-408
    • Mizuuchi, M.1    Mizuuchi, K.2
  • 46
    • 0342934743 scopus 로고
    • Structural domains in phase Mu transposase: Identification of the site-specific DNA-binding domain
    • Nakayama, C. Treplow, D.B. and Harshey, R.M. (1987) Structural domains in phase Mu transposase: identification of the site-specific DNA-binding domain. Proc. Natl Acad. Sci. USA, 84, 1809-1813.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1809-1813
    • Nakayama, C.1    Treplow, D.B.2    Harshey, R.M.3
  • 47
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A. Sharp, K. and Honig, B. (1991) Protein folding and association: insights from interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet., 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 49
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance geometry-dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. and Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance geometry-dynamical simulated annealing calculations. FEBS Lett., 229, 317-323.
    • (1988) FEBS Lett. , vol.229 , pp. 317-323
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 50
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C.O. and Sauer, R.T. (1992) Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem., 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 51
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
    • Rice, P.A. and Mizuuchi, K. (1995) Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell, 82, 209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.A.1    Mizuuchi, K.2
  • 53
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90°
    • Schultz, S.C., Shields, G.C. and Steitz, T.A. (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science, 253, 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 54
    • 0028173030 scopus 로고
    • Crystal structure of LacI member, PurR, bound to DNA: Minor groove binding by α helices
    • Schumacher, M.A., Choi, K.Y., Zalkin, H. and Brennan, R.G. (1994) Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by α helices. Science, 266, 763-770.
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 55
    • 0347610773 scopus 로고
    • An empirical correlation between protein backbone conformation and Cα and Cβ chemical shifts
    • Spera, S. and Bax, A. (1991) An empirical correlation between protein backbone conformation and Cα and Cβ chemical shifts. J. Am. Chem. Soc., 113, 5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 56
    • 0029976830 scopus 로고    scopus 로고
    • Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator
    • Spronk, C.A.E.M., Slijper, M., van Boom, J.H., Kaptein, R. and Boelens, R. (1996) Formation of the hinge helix in the lac repressor is induced upon binding to the lac operator. Nature Struct. Biol., 3, 916-919.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 916-919
    • Spronk, C.A.E.M.1    Slijper, M.2    Van Boom, J.H.3    Kaptein, R.4    Boelens, R.5
  • 57
    • 0023663468 scopus 로고
    • Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA
    • Surette, M.G., Buch, S.J. and Chaconas, G. (1987) Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell, 49, 253-262.
    • (1987) Cell , vol.49 , pp. 253-262
    • Surette, M.G.1    Buch, S.J.2    Chaconas, G.3
  • 58
    • 0024433737 scopus 로고
    • Action at a distance in Mu DNA transposition: An enhancer-like element is the site of action of supercoiling relief activity by integration host factor (IHF)
    • Surette, M.G., Lavoie, B.D. and Chaconas, G. (1989) Action at a distance in Mu DNA transposition: an enhancer-like element is the site of action of supercoiling relief activity by integration host factor (IHF). EMBO J., 8, 3483-3489.
    • (1989) EMBO J. , vol.8 , pp. 3483-3489
    • Surette, M.G.1    Lavoie, B.D.2    Chaconas, G.3
  • 59
    • 0028152571 scopus 로고
    • 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotope labeling
    • Vuister, G.W., Kim, S.-J., Wu, C. and Bax, A. (1994) 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotope labeling. J. Am. Chem. Soc., 116, 9206-9210.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9206-9210
    • Vuister, G.W.1    Kim, S.-J.2    Wu, C.3    Bax, A.4
  • 60
    • 0028034518 scopus 로고
    • Characterization of a region in phage Mu transposase that is involved in interaction with MuB protein
    • Wu, Z. and Chaconas, G. (1994) Characterization of a region in phage Mu transposase that is involved in interaction with MuB protein. J. Chem. Biol., 269, 28829-28833.
    • (1994) J. Chem. Biol. , vol.269 , pp. 28829-28833
    • Wu, Z.1    Chaconas, G.2
  • 61
    • 0029151254 scopus 로고
    • A novel DNA binding and nuclease activity in domain III of Mu transposase: Evidence for a catalytic region involved in donor cleavage
    • Wu, Z. and Chaconas, G. (1995) A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage. EMBO J., 14, 3835-3843.
    • (1995) EMBO J. , vol.14 , pp. 3835-3843
    • Wu, Z.1    Chaconas, G.2
  • 62
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang, W. and Steitz, T.A. (1995) Recombining the structures of HIV integrase, RuvC and RNase H. Structure, 3, 131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 63
    • 0025889778 scopus 로고
    • Transposase contacts with Mu DNA ends
    • ZOU, A., Leung, P.C. and Harshey, R.M. (1991) Transposase contacts with Mu DNA ends. J. Biol. Chem., 266, 20476-20482.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20476-20482
    • Zou, A.1    Leung, P.C.2    Harshey, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.