메뉴 건너뛰기




Volumn 343, Issue 1, 2004, Pages 115-136

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

Author keywords

DNA replication; helicases; motor proteins; protein ssDNA interactions; quantitative fluorescence titrations

Indexed keywords

DNA B; HELICASE; OLIGOMER; PURINE; REPA HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 4644321099     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.021     Document Type: Article
Times cited : (23)

References (56)
  • 3
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • T.M. Lohman, and K.P. Bjornson Mechanisms of helicase-catalyzed DNA unwinding Annu. Rev. Biochem. 65 1996 169 214
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 4
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: Structures and properties of isolated helicases
    • P.H. von Hippel, and E. Delagoutte Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: structures and properties of isolated helicases Quart. Rev. Biophys. 35 2002 431 478
    • (2002) Quart. 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
    • P.H. von Hippel, and E. Delagoutte Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: integration of helicases into cellular processes Quart. Rev. Biophys. 36 2003 1 69
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 1-69
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 7
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • W. Bujalowski, M.M. Klonowska, and M.J. Jezewska Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein J. Biol. Chem. 269 1994 31350 31358
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 8
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork. Recognition and structure
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork. Recognition and structure Biochemistry 37 1998 3116 3136
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 9
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • E.H. Egelman, X. Yu, R. Wild, M.M. Hingorani, and S.S. Patel Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases Proc. Natl Acad. Sci. USA 92 1995 3869 3873
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 10
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • F. Dong, E.P. Gogol, and P.H. von Hippel The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate J. Biol. Chem. 270 1995 7462 7473
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 11
    • 0017806122 scopus 로고
    • Replication of the nonconjugative plasmid RSF1010 in Escherichia coli K-12
    • J. De Gaaf, J.H. Crossa, F. Heffron, and S. Falkow Replication of the nonconjugative plasmid RSF1010 in Escherichia coli K-12 J. Bacteriol. 134 1978 1117 1122
    • (1978) J. Bacteriol. , vol.134 , pp. 1117-1122
    • De Gaaf, J.1    Crossa, J.H.2    Heffron, F.3    Falkow, S.4
  • 12
    • 0015964919 scopus 로고
    • Molecular nature of two nonconjugative plasmids carrying drug resistance genes
    • P. Guerry, J. van Embden, and S. Falkow Molecular nature of two nonconjugative plasmids carrying drug resistance genes J. Bacteriol. 117 1974 987 997
    • (1974) J. Bacteriol. , vol.117 , pp. 987-997
    • Guerry, P.1    Van Embden, J.2    Falkow, S.3
  • 14
    • 0030993427 scopus 로고    scopus 로고
    • Crysta;ization and preliminary crystallographic and electron microscopy study of bacterial DNA helicase (RSF1010 RepA)
    • D. Roleke, H. Hoier, C. Bartsch, P. Umbach, E. Scherzinger, R. Lurz, and W. Saenger Crysta;ization and preliminary crystallographic and electron microscopy study of bacterial DNA helicase (RSF1010 RepA) Acta Crystallog. sect. D 53 1997 213 216
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 213-216
    • Roleke, D.1    Hoier, H.2    Bartsch, C.3    Umbach, P.4    Scherzinger, E.5    Lurz, R.6    Saenger, W.7
  • 15
    • 0035936698 scopus 로고    scopus 로고
    • Crystal structure of the hexameric helicase RepA of plasmid RSF1010
    • T. Niedenzu, D. Roleke, S.E. Bains, and W. Saenger Crystal structure of the hexameric helicase RepA of plasmid RSF1010 J. Mol. Biol. 306 2001 479 487
    • (2001) J. Mol. Biol. , vol.306 , pp. 479-487
    • Niedenzu, T.1    Roleke, D.2    Bains, S.E.3    Saenger, W.4
  • 16
    • 0034613097 scopus 로고    scopus 로고
    • Interaction of different oligomeric states of hexameric DNA-helicase RepA with single-stranded DNA studied by analytical ultracentrifugation
    • H. Xu, J. Frank, J.F. Holzwarth, W. Saenger, and J. Behlke Interaction of different oligomeric states of hexameric DNA-helicase RepA with single-stranded DNA studied by analytical ultracentrifugation FEBS Letters 482 2000 180 184
    • (2000) FEBS Letters , vol.482 , pp. 180-184
    • Xu, H.1    Frank, J.2    Holzwarth, J.F.3    Saenger, W.4    Behlke, J.5
  • 17
    • 0035912866 scopus 로고    scopus 로고
    • Interactions of fluorescence labeled single-stranded DNA with hexameric DNA-helicase RepA: A photon and fluorescence correlation spectroscopy studies
    • H. Xu, J. Frank, U. Trier, S. Hammer, W. Schroder, and J. Behlke Interactions of fluorescence labeled single-stranded DNA with hexameric DNA-helicase RepA: a photon and fluorescence correlation spectroscopy studies Biochemistry 40 2001 7211 7218
    • (2001) Biochemistry , vol.40 , pp. 7211-7218
    • Xu, H.1    Frank, J.2    Trier, U.3    Hammer, S.4    Schroder, W.5    Behlke, J.6
  • 18
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • W. Bujalowski, and M.J. Jezewska Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer Biochemistry 34 1995 8513 8519
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 19
    • 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
    • M.J. Jezewska, U.-S. Kim, and W. Bujalowski Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer Biochemistry 35 1996 2129 2145
    • (1996) Biochemistry , vol.35 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 20
    • 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
    • M.J. Jezewska, and W. Bujalowski 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 1996 2117 2128
    • (1996) Biochemistry , vol.35 , pp. 2117-2128
    • Jezewska, M.J.1    Bujalowski, W.2
  • 21
    • 0030747747 scopus 로고    scopus 로고
    • Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with replication fork
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with replication fork Biochemistry 36 1997 10320 10326
    • (1997) Biochemistry , vol.36 , pp. 10320-10326
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 22
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding of the E. coli primary replicative helicase DnaB protein
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Functional and structural heterogeneity of the DNA binding of the E. coli primary replicative helicase DnaB protein J. Biol. Chem. 273 1998 9058 9069
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 23
    • 0032562822 scopus 로고    scopus 로고
    • Does ssDNA pass through the inner channel of the protein hexamer in the complex with the E. coli DnaB helicase? Fluorescence energy transfer studies
    • M.J. Jezewska, S. Rajendran, D. Bujalowska, and W. Bujalowski Does ssDNA pass through the inner channel of the protein hexamer in the complex with the E. coli DnaB helicase? Fluorescence energy transfer studies J. Biol. Chem. 273 1998 10515 10529
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 24
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork. Recognition and structure
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork. Recognition and structure Biochemistry 37 1998 3116 3136
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 25
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • W. Bujalowski, and M.M. Klonowska Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs Biochemistry 32 1993 5888 5900
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 26
    • 0029813340 scopus 로고    scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors
    • M.J. Jezewska, U.-S. Kim, and W. Bujalowski Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors Biophys. J. 71 1996 2075 2086
    • (1996) Biophys. J. , vol.71 , pp. 2075-2086
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 27
    • 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
    • W. Bujalowski, and M.J. Jezewska 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 2000 831 852
    • (2000) J. Mol. Biol. , vol.295 , pp. 831-852
    • Bujalowski, W.1    Jezewska, M.J.2
  • 28
    • 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
    • S. Rajendran, M.J. Jezewska, and W. Bujalowski 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 2000 773 795
    • (2000) J. Mol. Biol. , vol.303 , pp. 773-795
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 29
    • 0034623050 scopus 로고    scopus 로고
    • Escherichia coli helicase PriA protein-single stranded DNA complex
    • M. Jezewska, S. Rajendran, and W. Bujalowski Escherichia coli helicase PriA protein-single stranded DNA complex J. Biol. Chem. 275 2000 27865 27873
    • (2000) J. Biol. Chem. , vol.275 , pp. 27865-27873
    • Jezewska, M.1    Rajendran, S.2    Bujalowski, W.3
  • 30
    • 0034730112 scopus 로고    scopus 로고
    • Interactions of Escherichia coli replicative helicase PriA protein with single-stranded DNA
    • M. Jezewska, S. Rajendran, and W. Bujalowski Interactions of Escherichia coli replicative helicase PriA protein with single-stranded DNA Biochemistry 39 2000 10454 10467
    • (2000) Biochemistry , vol.39 , pp. 10454-10467
    • Jezewska, M.1    Rajendran, S.2    Bujalowski, W.3
  • 31
    • 0026351773 scopus 로고
    • Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: Spectroscopic approaches to monitor binding
    • T.M. Lohman, and W. Bujalowski Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding Methods Enzymol. 208 1991 258 290
    • (1991) Methods Enzymol. , vol.208 , pp. 258-290
    • Lohman, T.M.1    Bujalowski, W.2
  • 32
    • 0030888470 scopus 로고    scopus 로고
    • Quantitative analysis of ligand-macromolecule interactions using differential quenching of the ligand fluorescence to monitor the binding
    • M.J. Jezewska, and W. Bujalowski Quantitative analysis of ligand-macromolecule interactions using differential quenching of the ligand fluorescence to monitor the binding Biophys. Chem. 64 1997 253 269
    • (1997) Biophys. Chem. , vol.64 , pp. 253-269
    • Jezewska, M.J.1    Bujalowski, W.2
  • 34
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein
    • R. Galletto, S. Rajendran, and W. Bujalowski Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein Biochemistry 39 2000 12959 12969
    • (2000) Biochemistry , vol.39 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 35
    • 0035916918 scopus 로고    scopus 로고
    • Interactions of the 8-kDa domain of rat DNA polymerase β with DNA
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Interactions of the 8-kDa domain of rat DNA polymerase β with DNA Biochemistry 40 2001 3295 3307
    • (2001) Biochemistry , vol.40 , pp. 3295-3307
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 36
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Cooperative and noncooperative binding of large ligands to a one-dimensional homogeneous lattice
    • J.D. McGhee, and P.H. von Hippel Theoretical aspects of DNA-protein interactions: cooperative and noncooperative binding of large ligands to a one-dimensional homogeneous lattice J. Mol. Biol. 86 1974 469 489
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Von Hippel, P.H.2
  • 37
    • 0018196563 scopus 로고
    • Cooperative and non-cooperative binding of large ligands to a finite one-dimensional lattice. A model for ligand-oligonucleotide interactions
    • I.R. Epstein Cooperative and non-cooperative binding of large ligands to a finite one-dimensional lattice. A model for ligand-oligonucleotide interactions Biophys. Chem. 8 1978 327 339
    • (1978) Biophys. Chem. , vol.8 , pp. 327-339
    • Epstein, I.R.1
  • 38
    • 0024730670 scopus 로고
    • On the cooperative binding of large ligands to a one-dimensional homogeneous lattice: The generalized three-state lattice model
    • W. Bujalowski, T.M. Lohman, and C.F. Anderson On the cooperative binding of large ligands to a one-dimensional homogeneous lattice: the generalized three-state lattice model Biopolymers 28 1989 1637 1643
    • (1989) Biopolymers , vol.28 , pp. 1637-1643
    • Bujalowski, W.1    Lohman, T.M.2    Anderson, C.F.3
  • 39
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • M.T. Record, T.M. Lohman, and P.L. deHaseth Ion effects on ligand-nucleic acid interactions J. Mol. Biol. 107 1976 145 158
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, M.T.1    Lohman, T.M.2    Dehaseth, P.L.3
  • 40
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • M.T. Record Jr, C.F. Anderson, and T.M. Lohman Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity Quart. Rev. Biophys. 11 1978 103 178
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 44
    • 0032509151 scopus 로고    scopus 로고
    • Transition between different binding modes in rat DNA polymerase β-ssDNA complexes
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Transition between different binding modes in rat DNA polymerase β-ssDNA complexes J. Mol. Biol. 284 1998 1113 1131
    • (1998) J. Mol. Biol. , vol.284 , pp. 1113-1131
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 45
    • 0032553313 scopus 로고    scopus 로고
    • Human DNA polymerase β recognizes single-stranded DNA using two different binding modes
    • S. Rajendran, M.J. Jezewska, and W. Bujalowski Human DNA polymerase β recognizes single-stranded DNA using two different binding modes J. Biol. Chem. 273 1998 31021 31031
    • (1998) J. Biol. Chem. , vol.273 , pp. 31021-31031
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 46
    • 0017873807 scopus 로고
    • Base stacking in a fluorescent dinucleotiside monophosphate: εapεA
    • B.M. Baker, J. Vanderkooi, and N.R. Kallenbach Base stacking in a fluorescent dinucleotiside monophosphate: εApεA Biopolymers 17 1978 1361 1372
    • (1978) Biopolymers , vol.17 , pp. 1361-1372
    • Baker, B.M.1    Vanderkooi, J.2    Kallenbach, N.R.3
  • 47
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • H. Edelhoch Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6 1967 1948 1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 48
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 50
    • 36849119614 scopus 로고
    • Polarisation of the luminescence of phenanthrene
    • T. Azumi, and S.P. McGlynn Polarisation of the luminescence of phenanthrene J. Chem. Phys. 37 1962 2413 2420
    • (1962) J. Chem. Phys. , vol.37 , pp. 2413-2420
    • Azumi, T.1    McGlynn, S.P.2
  • 51
    • 0028207331 scopus 로고
    • Structural characteristics of the nucleotide binding site of the E. coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs
    • W. Bujalowski, and M.M. Klonowska Structural characteristics of the nucleotide binding site of the E. coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs Biochemistry 33 1994 4682 4694
    • (1994) Biochemistry , vol.33 , pp. 4682-4694
    • Bujalowski, W.1    Klonowska, M.M.2
  • 52
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • W. Stafford III Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile Anal. Biochem. 203 1992 295 301
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford III, W.1
  • 53
    • 0035814804 scopus 로고    scopus 로고
    • Sedimentation studies reveal a direct role of phosphorylation in Smad3:Smad4 homo- and hetero-dimerization
    • J.J. Correia, B.M. Chacko, S.S. Lam, and K. Lin Sedimentation studies reveal a direct role of phosphorylation in Smad3:Smad4 homo- and hetero-dimerization Biochemistry 40 2001 1473 1482
    • (2001) Biochemistry , vol.40 , pp. 1473-1482
    • Correia, J.J.1    Chacko, B.M.2    Lam, S.S.3    Lin, K.4
  • 54
    • 0037616144 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex
    • R. Galletto, M.J. Jezewska, and W. Bujalowski Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex J. Mol. Biol. 329 2003 441 465
    • (2003) J. Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.