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Volumn 48, Issue 44, 2009, Pages 10620-10636

Mechanisms of interactions of the nucleotide cofactor with the RepA protein of plasmid RSF1010. Binding dynamics studied using the fluorescence stopped-flow method

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DYNAMICS; COFACTORS; CONFORMATIONAL CHANGE; CONFORMATIONAL EQUILIBRIUM; CONFORMATIONAL TRANSITIONS; DNA BINDING SITE; HELICASES; HEXAMERIC HELICASES; HEXAMERS; INITIAL STAGES; INTERNAL TRANSITIONS; NUCLEOTIDE BINDING; NUCLEOTIDE-BINDING SITES; PARTIAL EQUILIBRIUM; PHOSPHATE GROUP; POSITIVE CHANGES; SINGLE-STRANDED DNA; STABILIZING INTERACTIONS; STOPPED-FLOW METHOD; THREE-STEP PROCESS;

EID: 70449436543     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900940q     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 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
  • 2
    • 0023654911 scopus 로고
    • Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro
    • Baker, T. A., Funnell, B. E., and Kornberg, A. (1987) Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro. J. Biol. Chem. 262, 6877-6885.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6877-6885
    • Baker, T.A.1    Funnell, B.E.2    Kornberg, A.3
  • 4
    • 0036880196 scopus 로고    scopus 로고
    • Helicase Mechanisms and the Coupling of Helicases Within Macromolecular Machines. Part I: Structures and Properties of Isolated Helicases
    • von Hippel, P. H., and Delagoutte, E. (2002) Helicase Mechanisms and the Coupling of Helicases Within Macromolecular Machines. Part I: Structures and Properties of Isolated Helicases. Q. Rev. Biophys. 35, 431-478.
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 431-478
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 5
    • 0037294467 scopus 로고    scopus 로고
    • Helicase Mechanisms and the Coupling of Helicases Within Macromolecular Machines. Part II: Integration of Helicases into Cellular Processes
    • von Hippel, P. H., and Delagoutte, E. (2003) Helicase Mechanisms and the Coupling of Helicases Within Macromolecular Machines. Part II: Integration of Helicases Into Cellular Processes. Q. Rev. Biophys. 36, 1-69.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 1-69
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 6
    • 34249950228 scopus 로고    scopus 로고
    • Non-Replicative Helicases at the Replication Fork
    • Heller, R. C., and Marians, K. J. (2007) Non-Replicative Helicases at the Replication Fork. DNA Repair 6, 945-952.
    • (2007) DNA Repair , vol.6 , pp. 945-952
    • Heller, R.C.1    Marians, K.J.2
  • 7
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB Replication Protein Is a DNA Helicase
    • LeBowitz, J. H., and McMacken, R. (1986) The Escherichia coli dnaB Replication Protein Is a DNA Helicase. J. Biol. Chem. 261, 4738-4748.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 8
    • 0015964919 scopus 로고
    • Molecular Nature of Two Nonconjugative Plasmids Carrying Drug Resistance Genes
    • Guerry, P., van Embden, J., and Falkow, S. (1974) Molecular Nature of Two Nonconjugative Plasmids Carrying Drug Resistance Genes. J. Bacteriol. 117, 987-997.
    • (1974) J. Bacteriol. , vol.117 , pp. 987-997
    • Guerry, P.1    Van Embden, J.2    Falkow, S.3
  • 9
    • 0017806122 scopus 로고
    • Replication of the nonconjugative plasmid RSF1010 in Escherichia coli K-12
    • De Gaaf, J., Crossa, J. H., Heffron, F., and Falkow, S. (1978) Replication of the Nonconjugative Plasmid RSF1010 in Escherichia coli K-12. J. Bacteriol. 134, 1117-1122. (Pubitemid 8354535)
    • (1978) Journal of Bacteriology , vol.134 , Issue.3 , pp. 1117-1122
    • De Graaff, J.1    Crosa, J.H.2    Heffron, F.3    Falkow, S.4
  • 11
    • 0035936698 scopus 로고    scopus 로고
    • Crystal Structure of the Hexameric Helicase RepA of Plasmid RSF1010
    • Niedenzu, T., Roleke, D., Bains, Scherzinger, E., and Saenger, W. (2001) Crystal Structure of the Hexameric Helicase RepA of Plasmid RSF1010. J. Mol. Biol. 306, 479-487.
    • (2001) J. Mol. Biol. , vol.306 , pp. 479-487
    • Niedenzu, T.1    Roleke, D.2    Bains3    Scherzinger, E.4    Saenger, W.5
  • 12
    • 4644321099 scopus 로고    scopus 로고
    • Interactions of the RepA helicase hexamer of plasmid RSF1010 with the ssDNA. Quantitative Analysis of Stoichiometries, Intrinsic Affinities, Cooperativities, and Heterogeneity of the Total ssDNA-Binding Site
    • Jezewska, M. J., Galletto, R., and Bujalowski, W. (2004) Interactions of the RepA helicase hexamer of plasmid RSF1010 with the ssDNA. Quantitative Analysis of Stoichiometries, Intrinsic Affinities, Cooperativities, and Heterogeneity of the Total ssDNA-Binding Site. J. Mol. Biol. 343, 115-136.
    • (2004) J. Mol. Biol. , vol.343 , pp. 115-136
    • Jezewska, M.J.1    Galletto, R.2    Bujalowski, W.3
  • 13
    • 14844349014 scopus 로고    scopus 로고
    • Binding of Six Nucleotide Cofactors to the Hexameric Helicase RepA Protein of Plasmid RSF1010. I. Direct Evidence of Cooperative Interactions between the Nucleotide-Binding Sites of a Hexameric Helicase
    • Jezewska, M. J., Lucius, A. L., and Bujalowski, W. (2005) Binding of Six Nucleotide Cofactors to the Hexameric Helicase RepA Protein of Plasmid RSF1010. I. Direct Evidence of Cooperative Interactions Between the Nucleotide-Binding Sites of a Hexameric Helicase. Biochemistry 44, 3865-3876.
    • (2005) Biochemistry , vol.44 , pp. 3865-3876
    • Jezewska, M.J.1    Lucius, A.L.2    Bujalowski, W.3
  • 14
    • 14844342992 scopus 로고    scopus 로고
    • Binding of Six Nucleotide Cofactors to the Hexameric Helicase RepA Protein of Plasmid RSF1010. II. Base Specificity, Nucleotide Structure, Magnesium, and Salt Effect on the Cooperative Binding of the Cofactors
    • Jezewska, M. J., Lucius, A. L., and Bujalowski, W. (2005) Binding of Six Nucleotide Cofactors to the Hexameric Helicase RepA Protein of Plasmid RSF1010. II. Base Specificity, Nucleotide Structure, Magnesium, and Salt Effect on the Cooperative Binding of the Cofactors. Biochemistry 44, 3877-3890.
    • (2005) Biochemistry , vol.44 , pp. 3877-3890
    • Jezewska, M.J.1    Lucius, A.L.2    Bujalowski, W.3
  • 15
    • 0028046581 scopus 로고
    • Oligomeric Structure of Escherichia coli Primary Replicative Helicase DnaB Protein
    • Bujalowski, W., Klonowska, M. M., and Jezewska, M. J. (1994) Oligomeric Structure of Escherichia coli Primary Replicative Helicase DnaB Protein. J. Biol. Chem. 269, 31350-31358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 16
    • 0030052444 scopus 로고    scopus 로고
    • Binding of Escherichia coli Primary Replicative Helicase DnaB Protein to Single-Stranded DNA. Long-Range Allosteric Conformational Changes within the Protein Hexamer
    • Jezewska, M. J., Kim, U.-S., and Bujalowski, W. (1996) Binding of Escherichia coli Primary Replicative Helicase DnaB Protein to Single-Stranded DNA. Long-Range Allosteric Conformational Changes within the Protein Hexamer. Biochemistry 35, 2129-2145.
    • (1996) Biochemistry , vol.35 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 17
    • 0028905501 scopus 로고
    • The Phage T4-coded DNA Replication Helicase (gp41) Forms a Hexamer Upon Activation by Nucleoside Triphosphate
    • Dong, F., Gogol, E. P., and von Hippel, P. H. (1995) The Phage T4-coded DNA Replication Helicase (gp41) Forms a Hexamer Upon Activation By Nucleoside Triphosphate. J. Biol. Chem. 270, 7462-7473.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 18
    • 0026091055 scopus 로고
    • Structure and Assembly of the Escherichia coli Transcription Termination Factor Rho and Its Interactions with RNA. I. Cryoelectron Microscopy Studies
    • Gogol, E. P., Seifried, S. E., and von Hippel, P. H. (1991) Structure and Assembly of the Escherichia coli Transcription Termination Factor Rho and Its Interactions With RNA. I. Cryoelectron Microscopy Studies. J. Mol. Biol. 221, 1127-1138.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1127-1138
    • Gogol, E.P.1    Seifried, S.E.2    Von Hippel, P.H.3
  • 19
    • 26944435616 scopus 로고    scopus 로고
    • Organization of an Archaeal MCM Complex on DNA and Implications for Helicase Mechanisms
    • Trakselis, M. A., McGeoch, A. T., Laskey, R. A., and Bell, S. D. (2005) Organization of an Archaeal MCM Complex on DNA and Implications For Helicase Mechanisms. Nat. Struct. Mol. Biol. 12, 756-762.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 756-762
    • Trakselis, M.A.1    McGeoch, A.T.2    Laskey, R.A.3    Bell, S.D.4
  • 20
    • 0029039925 scopus 로고
    • Bacteriophage T7 Helicase/Primase Proteins Form Rings Around Single-Stranded DNA that Suggest a General Structure for Hexameric Helicases
    • Egelman, E. H., Yu, X., Wild, R., Hingorani, M. M., and Patel, S. S. (1995) Bacteriophage T7 Helicase/Primase Proteins Form Rings Around Single-Stranded DNA that Suggest a General Structure for Hexameric Helicases. Proc. Natl. Acad. Sci. U.S.A. 92, 3869-3873.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 21
    • 36749066641 scopus 로고    scopus 로고
    • Multiple Global Conformational States of the Hexameric RepA Helicase of Plasmid RSF1010 with Different ssDNA-Binding Capabilities Are Induced by Different Numbers of Bound Nucleotides. Analytical Ultracentrifugation and Dynamic Light Scattering Studies
    • Marcinowicz, A., Jezewska, M. J., and Bujalowski, W. (2008) Multiple Global Conformational States of the Hexameric RepA Helicase of Plasmid RSF1010 With Different ssDNA-Binding Capabilities Are Induced by Different Numbers of Bound Nucleotides. Analytical Ultracentrifugation and Dynamic Light Scattering Studies. J. Mol. Biol. 375, 386-408.
    • (2008) J. Mol. Biol. , vol.375 , pp. 386-408
    • Marcinowicz, A.1    Jezewska, M.J.2    Bujalowski, W.3
  • 22
    • 0014109212 scopus 로고
    • Spectroscopic Determination of Tryptophan and Tyrosine in Proteins
    • Edelhoch, H. (1967) Spectroscopic Determination of Tryptophan and Tyrosine in Proteins. Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 23
    • 0024448151 scopus 로고
    • Calculation of Protein Extinction Coefficients from Amino Acid Sequence Data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of Protein Extinction Coefficients from Amino Acid Sequence Data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 24
    • 0027214787 scopus 로고
    • Negative Cooperativity in the Binding of Nucleotides to E. coli Replicative Helicase DnaB Protein. Interactions with Fluorescent Nucleotide Analogs
    • Bujalowski, W., and Klonowska, M. M. (1993) Negative Cooperativity in the Binding of Nucleotides to E. coli Replicative Helicase DnaB Protein. Interactions with Fluorescent Nucleotide Analogs. Biochemistry 32, 5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 25
    • 0028207331 scopus 로고
    • Structural Characteristics of the Nucleotide Binding Site of E. coli Primary Replicative Helicase DnaB Protein. Studies with Ribose and Base-Modified Fluorescent Nucleotide Analogs
    • Bujalowski, W., and Klonowska, M. M. (1994) Structural Characteristics of the Nucleotide Binding Site of E. coli Primary Replicative Helicase DnaB Protein. Studies with Ribose and Base-Modified Fluorescent Nucleotide Analogs. Biochemistry 33, 4682-4694.
    • (1994) Biochemistry , vol.33 , pp. 4682-4694
    • Bujalowski, W.1    Klonowska, M.M.2
  • 26
    • 33745027664 scopus 로고    scopus 로고
    • The Escherichia coli PriA Helicase Has Two Nucleotide-Binding Sites Differing in Their Affinities for Nucleotide Cofactors. 1. Intrinsic Affinities, Cooperativities, and Base Specificity of Nucleotide Cofactor Binding
    • Lucius, A. L., Jezewska, M. J., and Bujalowski, W. (2006) The Escherichia coli PriA Helicase Has Two Nucleotide-Binding Sites Differing in Their Affinities for Nucleotide Cofactors. 1. Intrinsic Affinities, Cooperativities, and Base Specificity of Nucleotide Cofactor Binding. Biochemistry 45, 7202-7216.
    • (2006) Biochemistry , vol.45 , pp. 7202-7216
    • Lucius, A.L.1    Jezewska, M.J.2    Bujalowski, W.3
  • 27
    • 33745052089 scopus 로고    scopus 로고
    • Kinetic mechanisms of the nucleotide cofactor binding to the strong and weak nucleotide-binding site of the Escherichia coli PriA helicase. 2
    • DOI 10.1021/bi051827e
    • Lucius, A. L., Jezewska, M. J., Roychowdhury, A., and Bujalowski, W. (2006) Kinetic Mechanisms of the Nucleotide Cofactor Binding to the Strong and Weak Nucleotide-Binding Site of the Escherichia coli PriA Helicase. 2. Biochemistry 45, 7217-7236. (Pubitemid 43877410)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7217-7236
    • Lucius, A.L.1    Jezewska, M.J.2    Roychowdhury, A.3    Bujalowski, W.4
  • 28
    • 33745043254 scopus 로고    scopus 로고
    • Allosteric Interactions between the Nucleotide-Binding Sites and the ssDNA-Binding Site in the PriA Helicase-ssDNA Complex. 3
    • Lucius, A. L., Jezewska, M. J., and Bujalowski, W. (2006) Allosteric Interactions Between the Nucleotide-Binding Sites and the ssDNA-Binding Site in the PriA Helicase-ssDNA Complex. 3. Biochemistry 45, 7237-7255.
    • (2006) Biochemistry , vol.45 , pp. 7237-7255
    • Lucius, A.L.1    Jezewska, M.J.2    Bujalowski, W.3
  • 29
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein
    • DOI 10.1021/bi0012484
    • Galletto, R., Rajendran, S., and Bujalowski, W. (2000) Interactions of Nucleotide Cofactors with the Escherichia coli Replication Factor DnaC Protein. Biochemistry 39, 12959-12969. (Pubitemid 30825899)
    • (2000) Biochemistry , vol.39 , Issue.42 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 30
    • 0032480793 scopus 로고    scopus 로고
    • Characterization of the Nucleotide Binding Properties of SV40 T Antigen Using Fluorescent 3′(2′)-O-(2,4,6-Trinitrophenyl)adenine Nucleotide Analogs
    • Huang, S.-G., Weisshart, K., and Fanning, E. (1998) Characterization of the Nucleotide Binding Properties of SV40 T Antigen Using Fluorescent 3′(2′)-O-(2,4,6-Trinitrophenyl)adenine Nucleotide Analogs. Biochemistry 37, 15336-15344.
    • (1998) Biochemistry , vol.37 , pp. 15336-15344
    • Huang, S.-G.1    Weisshart, K.2    Fanning, E.3
  • 31
    • 0030030309 scopus 로고    scopus 로고
    • A General Method of Analysis of Ligand Binding to Competing Macromolecules Using the Spectroscopic Signal Originating from a Reference Macromolecule. Application to Escherichia coli Replicative Helicase DnaB Protein-Nucleic Acid Interactions
    • Jezewska, M. J., and Bujalowski, W. (1996) A General Method of Analysis of Ligand Binding to Competing Macromolecules Using the Spectroscopic Signal Originating from a Reference Macromolecule. Application to Escherichia coli Replicative Helicase DnaB Protein-Nucleic Acid Interactions. Biochemistry 35, 2117-2128.
    • (1996) Biochemistry , vol.35 , pp. 2117-2128
    • Jezewska, M.J.1    Bujalowski, W.2
  • 32
    • 0030747747 scopus 로고    scopus 로고
    • Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork
    • DOI 10.1021/bi970712a
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (1997) Strand Specificity in the Interactions of Escherichia coli Primary Replicative Helicase DnaB Protein with Replication Fork. Biochemistry 36, 10320-10326. (Pubitemid 27357744)
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10320-10326
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 33
    • 0032502678 scopus 로고    scopus 로고
    • Functional and Structural Heterogeneity of the DNA Binding of the E. coli Primary Replicative Helicase DnaB Protein
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (1998) Functional and Structural Heterogeneity of the DNA Binding of the E. coli Primary Replicative Helicase DnaB Protein. J. Biol. Chem. 273, 9058-9069.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 34
    • 0010108989 scopus 로고    scopus 로고
    • Quantitative Determination of Equilibrium Binding Isotherms for the Multiple Ligand-Macromolecule Interactions Using Spectroscopic Methods
    • (Gore, M. G., Ed.) Chapter 5 Oxford University Press, New York
    • Bujalowski, W., and Jezewska, M. J. (2000) Quantitative Determination of Equilibrium Binding Isotherms for the Multiple Ligand-Macromolecule Interactions Using Spectroscopic Methods. In Spectrophotometry and Spectrofluorimetry: A Practical Approach (Gore, M. G., Ed.) Chapter 5, pp 141-165, Oxford University Press, New York.
    • (2000) Spectrophotometry and Spectrofluorimetry: A Practical Approach , pp. 141-165
    • Bujalowski, W.1    Jezewska, M.J.2
  • 35
    • 33644632662 scopus 로고    scopus 로고
    • Thermodynamic and Kinetic Methods of Analyses of Protein-Nucleic Acid Interactions. From Simpler to More Complex Systems
    • Bujalowski, W. (2006) Thermodynamic and Kinetic Methods of Analyses of Protein-Nucleic Acid Interactions. From Simpler to More Complex Systems. Chem. Rev. 106, 556-606.
    • (2006) Chem. Rev. , vol.106 , pp. 556-606
    • Bujalowski, W.1
  • 37
    • 36849119614 scopus 로고
    • Polarisation of the Luminescence of Phenantrene
    • Azumi, T., and McGlynn, S. P. (1962) Polarisation of the Luminescence of Phenantrene. J. Chem. Phys. 37, 2413-2420.
    • (1962) J. Chem. Phys. , vol.37 , pp. 2413-2420
    • Azumi, T.1    McGlynn, S.P.2
  • 38
    • 0034723155 scopus 로고    scopus 로고
    • Kinetic Mechanism of the Single-Stranded DNA Recognition by Escherichia coli Replicative Helicase DnaB Protein. Application of the Matrix Projection Operator Technique to Analyze Stopped-Flow Kinetics
    • Bujalowski, W., and Jezewska, M. J. (2000) Kinetic Mechanism of the Single-Stranded DNA Recognition by Escherichia coli Replicative Helicase DnaB Protein. Application of the Matrix Projection Operator Technique to Analyze Stopped-Flow Kinetics. J. Mol. Biol. 295, 831-852.
    • (2000) J. Mol. Biol. , vol.295 , pp. 831-852
    • Bujalowski, W.1    Jezewska, M.J.2
  • 39
    • 0034634365 scopus 로고    scopus 로고
    • Multiple-step Kinetic Mechanism of DNA-independent ATP Binding and Hydrolysis by Escherichia coli Replicative Helicase DnaB Protein: Quantitative Analysis Using the Rapid Quench-flow Method
    • Rajendran, S., Jezewska, M. J., and Bujalowski, W. (2000) Multiple-step Kinetic Mechanism of DNA-independent ATP Binding and Hydrolysis by Escherichia coli Replicative Helicase DnaB Protein: Quantitative Analysis Using the Rapid Quench-flow Method. J. Mol. Biol. 303, 773-795.
    • (2000) J. Mol. Biol. , vol.303 , pp. 773-795
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 40
    • 4644283081 scopus 로고    scopus 로고
    • Multi-Step Sequential Mechanism of E. coli Helicase PriA Protein-ssDNA Interactions. Kinetics and Energetics of the Active ssDNA-Searching Site of the Enzyme
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2004) Multi-Step Sequential Mechanism of E. coli Helicase PriA Protein-ssDNA Interactions. Kinetics and Energetics of the Active ssDNA-Searching Site of the Enzyme. Biochemistry 43, 11002-11016.
    • (2004) Biochemistry , vol.43 , pp. 11002-11016
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 41
    • 0034728364 scopus 로고    scopus 로고
    • Kinetic Mechanism of Nucleotide Cofactor Binding to Escherichia coli Replicative Helicase DnaB Protein. Stopped-Flow Kinetic Studies Using Fluorescent, Ribose-, and Base-Modified Nucleotide Analog
    • Bujalowski, W., and Jezewska, M. J. (2000) Kinetic Mechanism of Nucleotide Cofactor Binding to Escherichia coli Replicative Helicase DnaB Protein. Stopped-Flow Kinetic Studies Using Fluorescent, Ribose-, and Base-Modified Nucleotide Analog. Biochemistry 39, 2106-2122.
    • (2000) Biochemistry , vol.39 , pp. 2106-2122
    • Bujalowski, W.1    Jezewska, M.J.2
  • 42
    • 0037118714 scopus 로고    scopus 로고
    • The E. coli Replication Factor DnaC Protein Exists in Two Conformations with Different Nucleotide Binding Capabilities. I. Determination of the Binding Mechanism Using ATP and ADP Fluorescent Analogues
    • Galletto, R., and Bujalowski, W. (2002) The E. coli Replication Factor DnaC Protein Exists in Two Conformations with Different Nucleotide Binding Capabilities. I. Determination of the Binding Mechanism Using ATP and ADP Fluorescent Analogues. Biochemistry 41, 8907-8920.
    • (2002) Biochemistry , vol.41 , pp. 8907-8920
    • Galletto, R.1    Bujalowski, W.2
  • 43
    • 0037118717 scopus 로고    scopus 로고
    • Kinetics of the E. coli Replication Factor DnaC Protein-Nucleotide Interactions. II. Fluorescence Anisotropy and Transient, Dynamic Quenching Stopped-Flow Studies of the Reaction Intermediates
    • Galletto, R., and Bujalowski, W. (2002) Kinetics of the E. coli Replication Factor DnaC Protein-Nucleotide Interactions. II. Fluorescence Anisotropy and Transient, Dynamic Quenching Stopped-Flow Studies of the Reaction Intermediates. Biochemistry 41, 8921-8934.
    • (2002) Biochemistry , vol.41 , pp. 8921-8934
    • Galletto, R.1    Bujalowski, W.2
  • 44
    • 0037036453 scopus 로고    scopus 로고
    • Dynamics of Gapped DNA Recognition by Human Polymerase β
    • Bujalowski, W., Jezewska, M. J., and Galletto, R. (2002) Dynamics of Gapped DNA Recognition by Human Polymerase β. J. Biol. Chem. 277, 20316-20327.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20316-20327
    • Bujalowski, W.1    Jezewska, M.J.2    Galletto, R.3
  • 45
    • 0034728364 scopus 로고    scopus 로고
    • Kinetic Mechanism of Nucleotide Cofactor Binding to Escherichia coli Replicative Helicase DnaB Protein. Stopped-Flow Kinetic Studies Using Fluorescent, Ribose-, and Base-Modified Nucleotide Analog
    • Bujalowski, W., and Jezewska, M. J. (2000) Kinetic Mechanism of Nucleotide Cofactor Binding to Escherichia coli Replicative Helicase DnaB Protein. Stopped-Flow Kinetic Studies Using Fluorescent, Ribose-, and Base-Modified Nucleotide Analog. Biochemistry 39, 2106-2122.
    • (2000) Biochemistry , vol.39 , pp. 2106-2122
    • Bujalowski, W.1    Jezewska, M.J.2
  • 46
    • 24044468582 scopus 로고    scopus 로고
    • Kinetics of Allosteric Conformational Transition of a Macromolecule Prior to Ligand Binding. Analysis of Stopped-Flow Kinetic Experiments
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2005) Kinetics of Allosteric Conformational Transition of a Macromolecule Prior to Ligand Binding. Analysis of Stopped-Flow Kinetic Experiments. Cell Biochem. Biophys. 42, 121-144.
    • (2005) Cell Biochem. Biophys. , vol.42 , pp. 121-144
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 47
    • 0037036453 scopus 로고    scopus 로고
    • Dynamics of Gapped DNA Recognition by Human Polymerase β
    • Bujalowski, W., Jezewska, M. J., and Galletto, R. (2002) Dynamics of Gapped DNA Recognition by Human Polymerase β. J. Biol. Chem. 277, 20316-20327.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20316-20327
    • Bujalowski, W.1    Jezewska, M.J.2    Galletto, R.3
  • 48
    • 7244228547 scopus 로고    scopus 로고
    • - Group and Magnesium on the Enzyme Binding to the Gapped DNAs with Different ssDNA Gaps
    • - Group and Magnesium on the Enzyme Binding to the Gapped DNAs with Different ssDNA Gaps. Cell Biochem. Biophys. 38, 125-160.
    • (2003) Cell Biochem. Biophys. , vol.38 , pp. 125-160
    • Jezewska, M.J.1    Galletto, R.2    Bujalowski, W.3
  • 49
    • 13444306219 scopus 로고    scopus 로고
    • Kinetic Mechanism of Rat Polymerase β-dsDNA Interactions. Fluorescence Stopped-Flow Analysis of the Cooperative Ligand Binding to a Two-Site One-Dimensional Lattice
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2005) Kinetic Mechanism of Rat Polymerase β-dsDNA Interactions. Fluorescence Stopped-Flow Analysis of the Cooperative Ligand Binding to a Two-Site One-Dimensional Lattice. Biochemistry 44, 1251-1267.
    • (2005) Biochemistry , vol.44 , pp. 1251-1267
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 53
    • 36248933691 scopus 로고    scopus 로고
    • Structure of the tertiary complex of the RepA hexameric helicase of plasmid RSF1010 with the ssDNA and nucleotide cofactors in solution
    • DOI 10.1021/bi700729k
    • Marcinowicz, A., Jezewska, M. J., Bujalowski, P. J., and Bujalowski, W. (2007) The Structure of the Tertiary Complex of the RepA Hexameric Helicase of Plasmid RSF1010 with the ssDNA and Nucleotide Cofactors in Solution. Biochemistry 46, 13279-13296. (Pubitemid 350136369)
    • (2007) Biochemistry , vol.46 , Issue.46 , pp. 13279-13296
    • Marcinowicz, A.1    Jezewska, M.J.2    Bujalowski, P.J.3    Bujalowski, W.4
  • 54
    • 33947470645 scopus 로고
    • The Effect of Solvent on Spectra. II. Correlation of Spectral Absorption Data with Z-Values
    • Kosower, E. M. (1958) The Effect of Solvent on Spectra. II. Correlation of Spectral Absorption Data with Z-Values. J. Am. Chem. Soc. 80, 3253-3260.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 3253-3260
    • Kosower, E.M.1
  • 56
    • 67349097766 scopus 로고    scopus 로고
    • Dynamics of the ssDNA Recognition by the RepA Hexameric Helicase of Plasmid RSF1010. Analyses Using Fluorescence Stopped-Flow Intensity and Anisotropy Methods
    • Andreeva, I. E., Szymanski, M. R., Jezewska, M. J., Galletto, R., and Bujalowski, W. (2009) Dynamics of the ssDNA Recognition by the RepA Hexameric Helicase of Plasmid RSF1010. Analyses Using Fluorescence Stopped-Flow Intensity and Anisotropy Methods. J. Mol. Biol. 388, 751-775.
    • (2009) J. Mol. Biol. , vol.388 , pp. 751-775
    • Andreeva, I.E.1    Szymanski, M.R.2    Jezewska, M.J.3    Galletto, R.4    Bujalowski, W.5


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