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Volumn 43, Issue 34, 2004, Pages 10988-11001

Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DNA; FLUORESCENCE; GENETIC ENGINEERING; MOLECULAR BIOLOGY; MONOMERS; OLIGOMERS; SEDIMENTATION;

EID: 4644257077     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049377y     Document Type: Article
Times cited : (17)

References (51)
  • 2
    • 0026777126 scopus 로고
    • Prokaryotic DNA replication
    • Marians, K. J. (1992) Prokaryotic DNA replication, Annu. Rev. Biochem. 61, 673-719.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 673-719
    • Marians, K.J.1
  • 3
    • 0032605883 scopus 로고    scopus 로고
    • PriA: At the crossroads of DNA replication and recombination
    • Marians, K. J. (1999) PriA: at the crossroads of DNA replication and recombination, Prog. Nucl. Acid. Res., Mol. Biol. 63, 39-67.
    • (1999) Prog. Nucl. Acid. Res., Mol. Biol. , vol.63 , pp. 39-67
    • Marians, K.J.1
  • 4
    • 85039816294 scopus 로고
    • Interactions of escherichia coli dnaB and dnaC (D) gene products in vitro
    • Wickner, S., and Hurwitz, J. (1973) Interactions of Escherichia coli dnaB and dnaC (D) Gene Products In Vitro, Proc. Natl. Acad. Sci. U.S.A. 72, 783-787.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 783-787
    • Wickner, S.1    Hurwitz, J.2
  • 5
    • 0028838404 scopus 로고
    • The speed of the escherichia coli fork in vivo depends on the DnaB-DnaC ratio
    • (a) Skarstad, K., and Wold, S. (1995) The Speed of the Escherichia coli fork in vivo depends on the DnaB-DnaC ratio, Mol. Microbiol. 17, 825-831.
    • (1995) Mol. Microbiol. , vol.17 , pp. 825-831
    • Skarstad, K.1    Wold, S.2
  • 6
    • 0016426540 scopus 로고
    • Genetic and phenotypic characterization of dnaC mutations
    • (b) Wechsler, J. (1975) Genetic and phenotypic characterization of dnaC mutations, J. Bacteriol. 121, 594-599.
    • (1975) J. Bacteriol. , vol.121 , pp. 594-599
    • Wechsler, J.1
  • 7
    • 0015178421 scopus 로고
    • Escherichia coli mutants temperature-sensitive for DNA synthesis
    • Wechsler, J., and Gross, J. D. (1971) Escherichia coli mutants temperature-sensitive for DNA synthesis, Mol. Gen. Genet. 113, 273-284.
    • (1971) Mol. Gen. Genet. , vol.113 , pp. 273-284
    • Wechsler, J.1    Gross, J.D.2
  • 8
    • 0027522357 scopus 로고
    • Molecular matchmakers
    • Sancar, A., and Hearst, J. E. (1993) Molecular matchmakers, Science 259, 1415-1420.
    • (1993) Science , vol.259 , pp. 1415-1420
    • Sancar, A.1    Hearst, J.E.2
  • 9
    • 0035977018 scopus 로고    scopus 로고
    • DnaA protein directs the binding of the DnaB protein in initiation of DNA replication
    • Marszalek, J., and Kaguni, J. M. (2001) DnaA protein directs the binding of the DnaB protein in initiation of DNA replication, J. Biol. Chem. 276, 44919-44925.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44919-44925
    • Marszalek, J.1    Kaguni, J.M.2
  • 10
    • 0024562458 scopus 로고
    • The dnaB-dnaC replication protein complex of escherichia coli. I. Formation and properties
    • Wahle, E., Lasken, R. S., and Kornberg, A. (1989) The dnaB-dnaC Replication Protein Complex of Escherichia coli. I. Formation and Properties, J. Biol. Chem. 264, 2463-2468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2463-2468
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 11
    • 0024520416 scopus 로고
    • The dnaB-dnaC replication protein complex of escherichia coli. II. Role of the complex in mobilizing dnaB functions
    • Wahle, E., Lasken, R. S., and Kornberg, A. (1989) The dnaB-dnaC Replication Protein Complex of Escherichia coli. II. Role of the Complex in Mobilizing dnaB Functions, J. Biol. Chem. 264, 2469-2475.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 12
    • 0027184103 scopus 로고
    • Assembly of the primosome of DNA replication in Escherichia coli
    • Allen, G. C., and Kornberg, A. (1991) Assembly of the primosome of DNA replication in Escherichia coli, J. Biol. Chem. 268, 19204-19209.
    • (1991) J. Biol. Chem. , vol.268 , pp. 19204-19209
    • Allen, G.C.1    Kornberg, A.2
  • 13
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the escherichia coli replication factor DnaC protein
    • Galletto, R., Rajendran, S., and Bujalowski, W. (2000) Interactions of Nucleotide Cofactors with the Escherichia coli Replication Factor DnaC Protein, Biochemistry 39, 12959-12969.
    • (2000) Biochemistry , vol.39 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 14
    • 0037118714 scopus 로고    scopus 로고
    • The escherichia 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 analogs
    • Galletto, R., and Bujalowski, W. (2002) The Escherichia 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 Analogs, Biochemistry 41, 8907-8920.
    • (2002) Biochemistry , vol.41 , pp. 8907-8920
    • Galletto, R.1    Bujalowski, W.2
  • 15
    • 0037118717 scopus 로고    scopus 로고
    • Kinetics of 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 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
  • 16
    • 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 the protein-protein interactions and the topology of the complex
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2003) Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on the protein-protein interactions and the topology of the complex, J. Mol. Biol. 329, 441-465.
    • (2003) J. Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 17
    • 0015894660 scopus 로고
    • Preparation and properties of 2′(or3′)-O-(2,4,6- trinitrophenyl)adenosine 5′-triphosphate, an analog of adenosine triphosphate
    • Hiratsuka, T., and Uchida, K. (1973) Preparation and properties of 2′(or3′)-O-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate, an analog of adenosine triphosphate, Biochim. Biophys. Acta 320, 635-647.
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 635-647
    • Hiratsuka, T.1    Uchida, K.2
  • 18
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 19
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to escherichia 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 Escherichia 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
  • 20
    • 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
    • Bujalowski, W., and Klonowska, M. M. (1994) 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, 4682-4694.
    • (1994) Biochemistry , vol.33 , pp. 4682-4694
    • Bujalowski, W.1    Klonowska, M.M.2
  • 21
    • 0028046581 scopus 로고
    • Oligomeric structure of escherichia coli primary replicative helicase DnaB protein
    • Bujalowski, W., and Klonowska, M. M.; Jezewska M. J. (1994) Oligomeric Structure of Escherichia coli Primary Replicative Helicase DnaB Protein, J. Biol. Chem. 269, 31359-31371.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31359-31371
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 22
    • 0029813340 scopus 로고    scopus 로고
    • Interactions of escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors
    • Jezewska, M. J., Kim, U.-S., and Bujalowski, W. (1997) Interactions of Escherichia coli Primary Replicative Helicase DnaB Protein with Nucleotide Cofactors, Biophys. J. 71, 2075-2086.
    • (1997) Biophys. J. , vol.71 , pp. 2075-2086
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 23
    • 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
  • 24
    • 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
  • 25
    • 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
  • 27
    • 0032478286 scopus 로고    scopus 로고
    • Complex of escherichia coli primary replicative helicase DnaB protein with a replication fork. Recognition and structure
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (1998) Complex of Escherichia coli Primary Replicative Helicase DnaB Protein with a Replication Fork. Recognition and Structure, Biochemistry 37, 3116-3136.
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 28
    • 0030064012 scopus 로고    scopus 로고
    • Global conformational transitions in E. coli primary replicative DnaB protein induced by ATP, ADP and single-stranded DNA binding
    • Jezewska, M. J., and Bujalowski, W. (1996) Global Conformational Transitions in E. coli Primary Replicative DnaB Protein Induced by ATP, ADP and Single-Stranded DNA Binding, J. Biol. Chem. 271, 4261-4265.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4261-4265
    • Jezewska, M.J.1    Bujalowski, W.2
  • 29
    • 0032509151 scopus 로고    scopus 로고
    • Transition between different binding modes in rat DNA polymerase β - ssDNA complexes
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (1998) Transition Between Different Binding Modes In Rat DNA Polymerase β - ssDNA Complexes, J. Mol. Biol. 284, 1113-1131.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1113-1131
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 30
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford, W., III. (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile, Anal. Biochem. 203, 295-301.
    • (1992) Anal. Biochem. , vol.203 , pp. 295-301
    • Stafford III, W.1
  • 31
    • 0035814804 scopus 로고    scopus 로고
    • Sedimentation studies reveal a direct role of phosphorylation in Smad3: Smad4 homo- and hetero-dimerization
    • Correia, J. J., Chacko, B. M., Lam, S. S., and Lin, K. (2001) Sedimentation studies reveal a direct role of phosphorylation in Smad3: Smad4 homo- and hetero-dimerization, Biochemistry 40, 1473-1482.
    • (2001) Biochemistry , vol.40 , pp. 1473-1482
    • Correia, J.J.1    Chacko, B.M.2    Lam, S.S.3    Lin, K.4
  • 34
    • 0000702636 scopus 로고
    • W. H. Freeman and Company, New York
    • Cantor, C. R., and Schimmel, P. R. (1980) in Biophysical Chemistry, Part II, pp 591-641, W. H. Freeman and Company, New York.
    • (1980) Biophysical Chemistry , Issue.PART II , pp. 591-641
    • Cantor, C.R.1    Schimmel, P.R.2
  • 35
    • 0023645239 scopus 로고
    • Structure of escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with DnaB protein
    • Nakayama, N., Arai, N., Bond, M. W., Miyajima, A., Kobori, J., and Arai, K. (1987) Structure of Escherichia coli dnaC. Identification of a Cysteine Residue Possibly Involved in Association with dnaB Protein, J. Biol. Chem. 262, 10475-10480.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10475-10480
    • Nakayama, N.1    Arai, N.2    Bond, M.W.3    Miyajima, A.4    Kobori, J.5    Arai, K.6
  • 36
    • 0018402815 scopus 로고
    • The calculation of partial specific volumes of proteins in 6 M guanidine hydrochloride
    • Lee, J. C., and Timasheff, S. N. (1979) The Calculation of Partial Specific Volumes of Proteins in 6 M Guanidine Hydrochloride, Methods Enzym. 61, 49-57.
    • (1979) Methods Enzym. , vol.61 , pp. 49-57
    • Lee, J.C.1    Timasheff, S.N.2
  • 37
    • 0000800911 scopus 로고
    • Hydration of macromolecules. III. Hydration of polypeptides
    • Kuntz, I. D. (1971). Hydration of Macromolecules. III. Hydration of Polypeptides, J. Am. Chem. Soc. 93, 514-515.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 514-515
    • Kuntz, I.D.1
  • 38
    • 0014349173 scopus 로고
    • Protein hydration. I. Binding sites
    • Bull, H. B., and Breese, K. (1968) Protein Hydration. I. Binding Sites. Arch. Biochem. Biophys. 128, 488-496.
    • (1968) Arch. Biochem. Biophys. , vol.128 , pp. 488-496
    • Bull, H.B.1    Breese, K.2
  • 39
    • 0028046581 scopus 로고
    • Close proximity of tryptophan residues and ATP-binding site in escherichia coli primary replicative helicase DnaB protein
    • Bujalowski, W., Klonowska, M. M., and Jezewska, M. J. (1994) Close Proximity of Tryptophan Residues and ATP-binding Site in 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
  • 42
    • 0017852960 scopus 로고
    • Intrinsic segmental flexibility of the S-1 moiety of myosin using single-headed myosin
    • Mendelson, R., and Cheung, P. H-C. (1978) Intrinsic Segmental Flexibility of the S-1 Moiety of Myosin Using Single-Headed Myosin, Biochemistry, 17, 2139-2148.
    • (1978) Biochemistry , vol.17 , pp. 2139-2148
    • Mendelson, R.1    Cheung, P.H.-C.2
  • 43
    • 0020356352 scopus 로고
    • The escherichia coli dnaC gene product. I. Overproduction of the dnaC proteins of escherichia coli and salmonella typhimurium by cloning into a high copy number plasmid
    • Kobori, J. A., and Kornberg, A. (1982) The Escherichia coli dnaC Gene Product. I. Overproduction of the dnaC Proteins of Escherichia coli and Salmonella Typhimurium by Cloning into a High Copy Number Plasmid, J. Biol. Chem. 257, 13757-13762.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13757-13762
    • Kobori, J.A.1    Kornberg, A.2
  • 44
    • 0020355756 scopus 로고
    • The escherichia coli dnaC gene product. II. Purification, physical properties, and role in replication
    • Kobori, J. A., and Kornberg, A. (1982) The Escherichia coli dnaC Gene Product. II. Purification, Physical Properties, and Role in Replication, J. Biol. Chem. 257, 13763-13769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13763-13769
    • Kobori, J.A.1    Kornberg, A.2
  • 45
    • 0035868712 scopus 로고    scopus 로고
    • The DnaB-DnaC complex: A structure based on dimers assembled around an occluded channel
    • Barcena, M., Ruiz, T., Donate, L. E., Brown, S. E., Dixon, N. E., Radermacher, M., and Carazo, J. M. (2001) The DnaB-DnaC complex: a structure based on dimers assembled around an occluded channel, EMBO J. 20, 1462-1468.
    • (2001) EMBO J. , vol.20 , pp. 1462-1468
    • Barcena, M.1    Ruiz, T.2    Donate, L.E.3    Brown, S.E.4    Dixon, N.E.5    Radermacher, M.6    Carazo, J.M.7
  • 46
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • Yu, X., Jezewska, M. J., Bujalowski, W., and Egelman, E. H. (1996) The Hexameric E. coli DnaB Helicase can Exist in Different Quaternary 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
  • 47
  • 48
    • 0015530373 scopus 로고
    • 2 marques avec le 1-sulfonyl-5-dimethyl-aminonaphthalene
    • 2 marques avec le 1-sulfonyl-5-dimethyl-aminonaphthalene, Eur. J. Biochem. 25, 20-32.
    • (1975) Eur. J. Biochem. , vol.25 , pp. 20-32
    • Brochon, J.C.1    Wahl, P.2
  • 50
    • 84984085914 scopus 로고
    • Time-dependent fluorescence depolarization and brownian rotational diffusion coefficients of macromolecules
    • Tao, T. (1969) Time-Dependent Fluorescence Depolarization and Brownian Rotational Diffusion Coefficients of Macromolecules, Biopolymers 8, 609-632.
    • (1969) Biopolymers , vol.8 , pp. 609-632
    • Tao, T.1
  • 51
    • 0023368482 scopus 로고
    • Fluorescence dynamics studies of troponin C
    • Norris, L., and Steiner R. F. (1987) Fluorescence Dynamics Studies of Troponin C, Biopolymers 26, 1189-1204.
    • (1987) Biopolymers , vol.26 , pp. 1189-1204
    • Norris, L.1    Steiner, R.F.2


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