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Volumn 90, Issue 4, 1997, Pages 635-647

Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; HELICASE; SINGLE STRANDED DNA;

EID: 0030740262     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80525-5     Document Type: Article
Times cited : (449)

References (49)
  • 1
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali, J.A., and Lohman, T.M. (1997). Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275, 377-380.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 2
    • 0027172508 scopus 로고
    • Escherichia coli Rep helicase unwinds DNA by an active mechanism
    • Amaratunga, M., and Lohman, T.M. (1993). Escherichia coli Rep helicase unwinds DNA by an active mechanism. Biochemistry 32, 6815-6820.
    • (1993) Biochemistry , vol.32 , pp. 6815-6820
    • Amaratunga, M.1    Lohman, T.M.2
  • 3
    • 0028138413 scopus 로고
    • Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer
    • Bjornson, K.P., Amaratunga, M., Moore, K.J.M., and Lohman, T.M. (1994). Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer. Biochemistry 33, 14306-14316.
    • (1994) Biochemistry , vol.33 , pp. 14306-14316
    • Bjornson, K.P.1    Amaratunga, M.2    Moore, K.J.M.3    Lohman, T.M.4
  • 4
    • 0030025650 scopus 로고    scopus 로고
    • Kinetic mechanism of DNA binding and DNA-induced dimerization of the Escherichia coli Rep helicase
    • Bjornson, K.P., Moore, K.J.M., and Lohman, T.M. (1996a). Kinetic mechanism of DNA binding and DNA-induced dimerization of the Escherichia coli Rep helicase. Biochemistry 35, 2268-2282.
    • (1996) Biochemistry , vol.35 , pp. 2268-2282
    • Bjornson, K.P.1    Moore, K.J.M.2    Lohman, T.M.3
  • 5
    • 0030298002 scopus 로고    scopus 로고
    • ATP hydrolysis stimulates binding and release of single stranded DNA from alternating subunits of the dimeric E. coli Rep helicase: Implications for ATP-driven helicase translocation
    • Bjornson, K.P., Wong, I., and Lohman, T.M. (1996b). ATP hydrolysis stimulates binding and release of single stranded DNA from alternating subunits of the dimeric E. coli Rep helicase: implications for ATP-driven helicase translocation. J. Mol. Biol. 263, 411-422.
    • (1996) J. Mol. Biol. , vol.263 , pp. 411-422
    • Bjornson, K.P.1    Wong, I.2    Lohman, T.M.3
  • 6
    • 10144248959 scopus 로고    scopus 로고
    • A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III
    • Brosh, B.M., and Matson, S.W. (1996). A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III. J. Biol. Chem. 277, 25360-25368.
    • (1996) J. Biol. Chem. , vol.277 , pp. 25360-25368
    • Brosh, B.M.1    Matson, S.W.2
  • 7
    • 0343069451 scopus 로고
    • The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry (New Haven, CT: Yale University)
    • Brünger, A. (1992). X-PLOR (Version 3.1) Manual. The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry (New Haven, CT: Yale University).
    • (1992) X-PLOR (Version 3.1) Manual
    • Brünger, A.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite programs for protein crystallography
    • Collaborative computational project number 4
    • CCP4. (1994). Collaborative computational project number 4. The CCP4 suite programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 9
    • 0025022318 scopus 로고
    • DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins
    • Chao, K., and Lohman, T.M. (1990). DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins. J. Biol. Chem. 265, 1067-1076.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1067-1076
    • Chao, K.1    Lohman, T.M.2
  • 10
    • 0026054936 scopus 로고
    • DNA-induced dimerization of the Escherichia coli Rep helicase
    • Chao, K., and Lohman, T.M. (1991). DNA-induced dimerization of the Escherichia coli Rep helicase. J. Mol. Biol. 221, 1165-1181.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1165-1181
    • Chao, K.1    Lohman, T.M.2
  • 11
    • 0026754531 scopus 로고
    • Analysis of the Escherichia coligenome: DNA sequence of the region from 84.5 to 86.5 minutes
    • Daniels, D.L., Plunkett, G., Burland, V., and Blattner, F.R. (1992). Analysis of the Escherichia coligenome: DNA sequence of the region from 84.5 to 86.5 minutes. Science 257, 771-778.
    • (1992) Science , vol.257 , pp. 771-778
    • Daniels, D.L.1    Plunkett, G.2    Burland, V.3    Blattner, F.R.4
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A., and Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 0026465663 scopus 로고
    • Xeroderma pigmentosum, Cockayne's syndrome, helicases, and DNA repair: What's the relationship?
    • Friedberg, E.G. (1992). Xeroderma pigmentosum, Cockayne's syndrome, helicases, and DNA repair: what's the relationship? Cell 71, 887-889.
    • (1992) Cell , vol.71 , pp. 887-889
    • Friedberg, E.G.1
  • 14
    • 0023089713 scopus 로고
    • Escherichia coli rep gene: Sequence of the gene, the encoded helicase, and its homology with uvrD
    • Gilchrist, C.A., and Denhardt, D.T. (1987). Escherichia coli rep gene: sequence of the gene, the encoded helicase, and its homology with uvrD. Nucleic Acids Res. 15, 465-475.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 465-475
    • Gilchrist, C.A.1    Denhardt, D.T.2
  • 15
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A.E., and Koonin, E.V. (1993). Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 16
    • 0028596398 scopus 로고
    • Transcription-coupled repair and human diseases
    • Hanawalt, P.C. (1994). Transcription-coupled repair and human diseases. Science 266, 1957-1958.
    • (1994) Science , vol.266 , pp. 1957-1958
    • Hanawalt, P.C.1
  • 17
    • 0019835096 scopus 로고
    • Theoretical aspects of translocation on DNA: Adenosine triphosphatase and treadmilling binding proteins
    • Hill, T.L., and Tsuchiya, T. (1981). Theoretical aspects of translocation on DNA: adenosine triphosphatase and treadmilling binding proteins. Proc. Natl. Acad. Sci. USA 78, 4796-4800.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4796-4800
    • Hill, T.L.1    Tsuchiya, T.2
  • 18
    • 0029960345 scopus 로고    scopus 로고
    • The movement of kinesin along microtubules
    • Howard, J. (1996). The movement of kinesin along microtubules. Annu. Rev. Physiol. 58, 703-729.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 703-729
    • Howard, J.1
  • 19
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones, T.A., and Thirup, S. (1986). Using known substructures in protein model building and crystallography. EMBO J. 5, 819-822.
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and 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
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to reproduce both detailed and schematic plots of protein structure
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to reproduce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0028237708 scopus 로고    scopus 로고
    • Structural determinant for activation of the α-subunit of a heterotrimeric G protein
    • Lambright, D.G., Noel, J.P., Hamm, H.E., and Sigler, P.B. (1996). Structural determinant for activation of the α-subunit of a heterotrimeric G protein. Nature 379, 621-628.
    • (1996) Nature , vol.379 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 24
    • 0016710698 scopus 로고
    • The Rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains
    • Lane, H.E.D., and Denhardt, D.T. (1975a). The Rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains. J. Mol. Biol. 97, 99-112.
    • (1975) J. Mol. Biol. , vol.97 , pp. 99-112
    • Lane, H.E.D.1    Denhardt, D.T.2
  • 25
    • 0016123202 scopus 로고
    • The rep mutation: III. Altered structure of the replicating Escherichia chromosome
    • Lane, H.E.D., and Denhardt, D.T. (1975b). The rep mutation: III. Altered structure of the replicating Escherichia chromosome. J. Bacteriol. 120, 805-814.
    • (1975) J. Bacteriol. , vol.120 , pp. 805-814
    • Lane, H.E.D.1    Denhardt, D.T.2
  • 26
    • 0026597376 scopus 로고
    • Escherichia coli DNA helicases: Mechanisms of DNA unwinding
    • Lohman, T.M. (1992). Escherichia coli DNA helicases: mechanisms of DNA unwinding. Mol. Microbiol. 6, 5-14.
    • (1992) Mol. Microbiol. , vol.6 , pp. 5-14
    • Lohman, T.M.1
  • 27
    • 0027518667 scopus 로고
    • Helicase-catalyzed DNA unwinding
    • Lohman, T.M. (1993). Helicase-catalyzed DNA unwinding. J. Biol. Chem. 268, 2269-2272.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2269-2272
    • Lohman, T.M.1
  • 28
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T.M., and Bjornson, K.P. (1996). Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 29
    • 0024328156 scopus 로고
    • Large-scale purification and characterization of the Escherichia coli rep gene product
    • Lohman, T.M., Chao, K., Green, J.M., Sage, S., and Runyon, G.T. (1989). Large-scale purification and characterization of the Escherichia coli rep gene product. J. Biol. Chem. 264, 10139-10147.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10139-10147
    • Lohman, T.M.1    Chao, K.2    Green, J.M.3    Sage, S.4    Runyon, G.T.5
  • 30
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A., and Murphy, M.E.P. (1994). Raster3D Version 2.0 - A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 31
    • 0028566711 scopus 로고
    • Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogs
    • Moore, K.J.M., and Lohman, T.M. (1994a). Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogs. Biochemistry 33, 14550-14564.
    • (1994) Biochemistry , vol.33 , pp. 14550-14564
    • Moore, K.J.M.1    Lohman, T.M.2
  • 32
    • 0028598302 scopus 로고
    • Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approach
    • Moore, K.J.M., and Lohman, T.M. (1994b). Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approach. Biochemistry 33, 14565-14578.
    • (1994) Biochemistry , vol.33 , pp. 14565-14578
    • Moore, K.J.M.1    Lohman, T.M.2
  • 35
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor elF-4A
    • Pause, A., and Sonenberg, N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor elF-4A. EMBO J. 11, 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 36
    • 0028606403 scopus 로고
    • Mechanisms of DNA excision repair
    • Sancar, A. (1994). Mechanisms of DNA excision repair. Science 266, 1954-1957.
    • (1994) Science , vol.266 , pp. 1954-1957
    • Sancar, A.1
  • 37
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R.M., and Steitz, T.A. (1992). Structure of the recA protein-ADP complex. Nature 355, 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 38
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I.T., and Steitz, T.A. (1992). The structure of the E coli recA protein monomer and polymer. Nature 355, 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 40
    • 0027955411 scopus 로고
    • Xeroderma pigmentosum and nucleotide excision repair
    • Tanaka, K., and Wood, R.D. (1994). Xeroderma pigmentosum and nucleotide excision repair. Trends Biol Sci. 19, 83-86.
    • (1994) Trends Biol Sci. , vol.19 , pp. 83-86
    • Tanaka, K.1    Wood, R.D.2
  • 41
    • 0001940082 scopus 로고
    • MAD phasing treatment of dispersive differences as isomorphous replacement information
    • Terwilliger, T.C. (1994). MAD phasing treatment of dispersive differences as isomorphous replacement information. Acta Crystallogr. D50, 17-23.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 17-23
    • Terwilliger, T.C.1
  • 42
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong, I., and Lohman, T.M. (1992). Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256, 350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 43
    • 0029836219 scopus 로고    scopus 로고
    • ATPase activity of Escherichia coli Rep helicase crosslinked to single-stranded DNA: Implications for ATP-driven helicase translocation
    • Wong, I., and Lohman, T.M. (1996). ATPase activity of Escherichia coli Rep helicase crosslinked to single-stranded DNA: implications for ATP-driven helicase translocation. Proc. Natl. Acad. Sci. USA 93, 10051-10056.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10051-10056
    • Wong, I.1    Lohman, T.M.2
  • 44
    • 0030945130 scopus 로고    scopus 로고
    • 2S) as revealed by site-specific inhibition with ADP-ALF4
    • 2S) as revealed by site-specific inhibition with ADP-ALF4. Biochemistry 36, 3115-3125.
    • (1997) Biochemistry , vol.36 , pp. 3115-3125
    • Wong, I.1    Lohman, T.M.2
  • 45
    • 0026646192 scopus 로고
    • DNA-induced dimerization of the Escherichia coli Rep helicase. Allosteric effects of single-stranded and duplex DNA
    • Wong, I., Chao, K.L., Bujalowski, W., and Lohman, T.M. (1992). DNA-induced dimerization of the Escherichia coli Rep helicase. Allosteric effects of single-stranded and duplex DNA. J. Biol. Chem. 267, 7596-7610.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7596-7610
    • Wong, I.1    Chao, K.L.2    Bujalowski, W.3    Lohman, T.M.4
  • 46
    • 0027237279 scopus 로고
    • Heterodimer formation between Escherichia coli Rep and UvrD proteins
    • Wong, I., Amaratunga, M., and Lohman, T.M. (1993). Heterodimer formation between Escherichia coli Rep and UvrD proteins. J. Biol. Chem. 268, 20386-20391.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20386-20391
    • Wong, I.1    Amaratunga, M.2    Lohman, T.M.3
  • 47
    • 0029882507 scopus 로고    scopus 로고
    • ATPase activity of Escherichia coli Rep helicase is dramatically dependent on DNA ligation and protein oligomeric states
    • Wong, I., Moore, K.J.M., Bjornson, K.P., Hsieh, J., and Lohman, T.M. (1996). ATPase activity of Escherichia coli Rep helicase is dramatically dependent on DNA ligation and protein oligomeric states. Biochemistry 35, 5726-5734.
    • (1996) Biochemistry , vol.35 , pp. 5726-5734
    • Wong, I.1    Moore, K.J.M.2    Bjornson, K.P.3    Hsieh, J.4    Lohman, T.M.5
  • 48
    • 0018353521 scopus 로고
    • Enzyme-catalyzed DNA unwinding studies on Escherichia coli Rep protein
    • Yarranton, G.T., and Getter, M.L. (1979). Enzyme-catalyzed DNA unwinding studies on Escherichia coli Rep protein. Proc. Natl. Acad. Sci. USA 76, 1658-1662.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1658-1662
    • Yarranton, G.T.1    Getter, M.L.2
  • 49
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quarternary states
    • Yu, X., Jezewska, M.J., Bujalowski, W., and Egelman, E.H. (1996). The hexameric E. coli DnaB helicase can exist in different quarternary states. J. Mol. Biol. 259, 7-14.
    • (1996) J. Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4


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