메뉴 건너뛰기




Volumn 43, Issue 10, 2008, Pages 1082-1093

Mesoscale modeling of multi-protein-DNA assemblies: The role of the catabolic activator protein in Lac-repressor-mediated looping

Author keywords

Boundary value problem; Elasticity; Free energy; Molecular biology; Rod; Transcription

Indexed keywords

ABS RESINS; BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; BOUNDARY VALUE PROBLEMS; DIFFERENTIAL EQUATIONS; DNA; ELASTICITY; ESCHERICHIA COLI; FREE ENERGY; GENES; INITIAL VALUE PROBLEMS; MOLECULAR BIOLOGY; ORGANIC ACIDS; OZONE WATER TREATMENT; RNA; TRANSCRIPTION;

EID: 56949101883     PISSN: 00207462     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijnonlinmec.2008.07.003     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0038298831 scopus 로고    scopus 로고
    • Theory of sequence-dependent DNA elasticity
    • Coleman B.D., Olson W.K., and Swigon D. Theory of sequence-dependent DNA elasticity. J. Chem. Phys. 118 (2003) 7127
    • (2003) J. Chem. Phys. , vol.118 , pp. 7127
    • Coleman, B.D.1    Olson, W.K.2    Swigon, D.3
  • 2
    • 0016732596 scopus 로고
    • Transmission of stability (telestability) in deoxyribonucleic acid
    • Burd J.F., Wartell R.M., Dodgson J.B., and Wells R.D. Transmission of stability (telestability) in deoxyribonucleic acid. J. Biol. Chem. 250 (1975) 5109
    • (1975) J. Biol. Chem. , vol.250 , pp. 5109
    • Burd, J.F.1    Wartell, R.M.2    Dodgson, J.B.3    Wells, R.D.4
  • 4
    • 33745595880 scopus 로고    scopus 로고
    • Modeling the Lac repressor-operator assembly: the influence of DNA looping on Lac repressor conformation
    • Swigon D., Coleman B.D., and Olson W.K. Modeling the Lac repressor-operator assembly: the influence of DNA looping on Lac repressor conformation. Proc. Natl. Acad. Sci. USA 103 (2006) 9879
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9879
    • Swigon, D.1    Coleman, B.D.2    Olson, W.K.3
  • 7
    • 0025025888 scopus 로고
    • Co-operative interactions between the catabolite gene activator protein and the lac repressor at the lactose promoter
    • Hudson J.M., and Fried M.G. Co-operative interactions between the catabolite gene activator protein and the lac repressor at the lactose promoter. J. Mol. Biol. 214 (1990) 381
    • (1990) J. Mol. Biol. , vol.214 , pp. 381
    • Hudson, J.M.1    Fried, M.G.2
  • 8
    • 0030582618 scopus 로고    scopus 로고
    • DNA looping and Lac repressor-CAP interaction
    • Fried G.M., and Hudson J.M. DNA looping and Lac repressor-CAP interaction. Science 274 (1996) 1930
    • (1996) Science , vol.274 , pp. 1930
    • Fried, G.M.1    Hudson, J.M.2
  • 9
    • 1642534356 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by CAP and Lac repressor
    • Balaeff A., Mahadevan L., and Schulten K. Structural basis for cooperative DNA binding by CAP and Lac repressor. Structure 12 (2004) 123
    • (2004) Structure , vol.12 , pp. 123
    • Balaeff, A.1    Mahadevan, L.2    Schulten, K.3
  • 10
    • 0037124326 scopus 로고    scopus 로고
    • Plasticity in protein-DNA recognition: Lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain
    • Kalodimos C.G., Bonvin A.M.J.J., Salinas R.K., Wechselberger R., Boelens R., and Kaptein R. Plasticity in protein-DNA recognition: Lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain. EMBO J. 21 (2002) 2866
    • (2002) EMBO J. , vol.21 , pp. 2866
    • Kalodimos, C.G.1    Bonvin, A.M.J.J.2    Salinas, R.K.3    Wechselberger, R.4    Boelens, R.5    Kaptein, R.6
  • 13
    • 0026796061 scopus 로고
    • DNA bending, flexibility, and helical repeat by cyclization kinetics
    • Crothers D.M., Drak J., Kahn J.D., and Levene S.D. DNA bending, flexibility, and helical repeat by cyclization kinetics. Methods Enzymol. 212 (1992) 3
    • (1992) Methods Enzymol. , vol.212 , pp. 3
    • Crothers, D.M.1    Drak, J.2    Kahn, J.D.3    Levene, S.D.4
  • 14
    • 0026642548 scopus 로고
    • Straightening out the bends in curved DNA
    • Hagerman P.J. Straightening out the bends in curved DNA. Biochem. Biophys. Acta 1131 (1992) 125
    • (1992) Biochem. Biophys. Acta , vol.1131 , pp. 125
    • Hagerman, P.J.1
  • 15
    • 0036283344 scopus 로고    scopus 로고
    • Sequence-dependent motions of DNA: a normal mode analysis at the base-pair level
    • Matsumoto A., and Olson W.K. Sequence-dependent motions of DNA: a normal mode analysis at the base-pair level. Biophys. J. 83 (2002) 22
    • (2002) Biophys. J. , vol.83 , pp. 22
    • Matsumoto, A.1    Olson, W.K.2
  • 17
    • 3042572330 scopus 로고    scopus 로고
    • Implications of the dependence of the elastic properties of DNA on nucleotide sequence
    • Olson W.K., Swigon D., and Coleman B.D. Implications of the dependence of the elastic properties of DNA on nucleotide sequence. Philos. Trans. R. Soc. Lond. A 362 (2004) 1403
    • (2004) Philos. Trans. R. Soc. Lond. A , vol.362 , pp. 1403
    • Olson, W.K.1    Swigon, D.2    Coleman, B.D.3
  • 18
    • 0029126044 scopus 로고
    • The assessment of the geometry of dinucleotide steps in double-helical DNA; a new local calculation scheme
    • El Hassan M.A., and Calladine C.R. The assessment of the geometry of dinucleotide steps in double-helical DNA; a new local calculation scheme. J. Mol. Biol. 251 (1995) 648
    • (1995) J. Mol. Biol. , vol.251 , pp. 648
    • El Hassan, M.A.1    Calladine, C.R.2
  • 19
    • 50249107536 scopus 로고    scopus 로고
    • Insights into the sequence-dependent macromolecular properties of DNA from base-pair level modeling
    • Voth G.A. (Ed), Taylor & Francis Group, LLC, London (Chapter 14)
    • Olson W.K., Colasanti A.V., Czapla L., and Zheng G. Insights into the sequence-dependent macromolecular properties of DNA from base-pair level modeling. In: Voth G.A. (Ed). Course-Graining of Condensed Phase and Biomolecular Systems (2008), Taylor & Francis Group, LLC, London 205-223 (Chapter 14)
    • (2008) Course-Graining of Condensed Phase and Biomolecular Systems , pp. 205-223
    • Olson, W.K.1    Colasanti, A.V.2    Czapla, L.3    Zheng, G.4
  • 20
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning G.S. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11 (1978) 179
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 179
    • Manning, G.S.1
  • 23
    • 56949086860 scopus 로고    scopus 로고
    • R. Courant, Differential and Integral Calculus, Blackie, London, vol. 2, 1936.
    • R. Courant, Differential and Integral Calculus, Blackie, London, vol. 2, 1936.
  • 24
    • 56949087264 scopus 로고    scopus 로고
    • J.H. White, in: M.S. Waterman (Ed.), Mathematical Methods for DNA Sequences, CRC Press, Boca Raton, FL, 1989, pp. 225.
    • J.H. White, in: M.S. Waterman (Ed.), Mathematical Methods for DNA Sequences, CRC Press, Boca Raton, FL, 1989, pp. 225.
  • 25
    • 0031969344 scopus 로고    scopus 로고
    • The elastic rod model for DNA and its application to the tertiary structure of DNA minicircles in mononucleosomes
    • Swigon D., Coleman B.D., and Tobias I. The elastic rod model for DNA and its application to the tertiary structure of DNA minicircles in mononucleosomes. Biophys. J. 74 (1998) 2515
    • (1998) Biophys. J. , vol.74 , pp. 2515
    • Swigon, D.1    Coleman, B.D.2    Tobias, I.3
  • 26
    • 33747623305 scopus 로고    scopus 로고
    • End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation
    • Möglich A., Joder K., and Kiefhaber T. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation. Proc. Natl. Acad. Sci. USA 103 (2006) 12394
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12394
    • Möglich, A.1    Joder, K.2    Kiefhaber, T.3
  • 30
    • 56949084667 scopus 로고    scopus 로고
    • H.W. Kuhn, A.W. Tucker, Nonlinear Programming, in: Proceedings of the 2nd Berkeley Symposium, University of California Press, Berkeley, CA, 1951, p. 481.
    • H.W. Kuhn, A.W. Tucker, Nonlinear Programming, in: Proceedings of the 2nd Berkeley Symposium, University of California Press, Berkeley, CA, 1951, p. 481.
  • 31
    • 34250683788 scopus 로고    scopus 로고
    • On bifurcations of equilibria of intrinsically curved, electrically charged, rod-like structures that model DNA molecules in solution
    • Biton Y.Y., Coleman B.D., and Swigon D. On bifurcations of equilibria of intrinsically curved, electrically charged, rod-like structures that model DNA molecules in solution. J. Elasticity 87 (2007) 187
    • (2007) J. Elasticity , vol.87 , pp. 187
    • Biton, Y.Y.1    Coleman, B.D.2    Swigon, D.3
  • 32
    • 0035595722 scopus 로고    scopus 로고
    • Extracting parameters for base-pair level models of DNA from molecular dynamics simulations
    • Gonzales O., and Maddocks J.H. Extracting parameters for base-pair level models of DNA from molecular dynamics simulations. Theor. Chem. Acc. 106 (2001) 76
    • (2001) Theor. Chem. Acc. , vol.106 , pp. 76
    • Gonzales, O.1    Maddocks, J.H.2
  • 33
    • 0037215722 scopus 로고    scopus 로고
    • Statistical mechanics of sequence-dependent circular DNA and its application for DNA cyclization
    • Zhang Y.L., and Crothers D.M. Statistical mechanics of sequence-dependent circular DNA and its application for DNA cyclization. Biophys. J. 84 (2003) 136
    • (2003) Biophys. J. , vol.84 , pp. 136
    • Zhang, Y.L.1    Crothers, D.M.2
  • 34
    • 33749243974 scopus 로고    scopus 로고
    • Sequence-dependent effects in the cyclization of short DNA
    • Czapla L., Swigon D., and Olson W.K. Sequence-dependent effects in the cyclization of short DNA. J. Chem. Theory Comput. 2 (2006) 685
    • (2006) J. Chem. Theory Comput. , vol.2 , pp. 685
    • Czapla, L.1    Swigon, D.2    Olson, W.K.3
  • 36
    • 0031002095 scopus 로고    scopus 로고
    • Conformation of Lac repressor tetramer in solution, bound and unbound to operator DNA
    • Ruben G.C., and Roos T.B. Conformation of Lac repressor tetramer in solution, bound and unbound to operator DNA. Microsc. Res. Tech. 36 (1997) 400
    • (1997) Microsc. Res. Tech. , vol.36 , pp. 400
    • Ruben, G.C.1    Roos, T.B.2
  • 37
    • 18744391399 scopus 로고    scopus 로고
    • Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation
    • Villa E., Balaeff A., and Schulten K. Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation. Proc. Natl. Acad. Sci., USA 102 (2005) 6783
    • (2005) Proc. Natl. Acad. Sci., USA , vol.102 , pp. 6783
    • Villa, E.1    Balaeff, A.2    Schulten, K.3
  • 38
    • 0029004903 scopus 로고
    • Crystal structure of Lac repressor core tetramer and its implications for DNA looping
    • Friedman A.M., Fischmann T.O., and Steitz T.A. Crystal structure of Lac repressor core tetramer and its implications for DNA looping. Science 268 (1995) 1721
    • (1995) Science , vol.268 , pp. 1721
    • Friedman, A.M.1    Fischmann, T.O.2    Steitz, T.A.3
  • 40
    • 0034089394 scopus 로고    scopus 로고
    • Closer view of the conformation of the Lac repressor bound to operator
    • Bell C.E., and Lewis M.A. Closer view of the conformation of the Lac repressor bound to operator. Nat. Struct. Biol. 7 (2000) 209
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 209
    • Bell, C.E.1    Lewis, M.A.2
  • 43
    • 0030033622 scopus 로고    scopus 로고
    • Mode of selectivity in cyclic AMP receptor protein-dependent promoters in Escherichia coli
    • Pyles E.A., and Lee J.C. Mode of selectivity in cyclic AMP receptor protein-dependent promoters in Escherichia coli. Biochemistry 35 (1996) 1162
    • (1996) Biochemistry , vol.35 , pp. 1162
    • Pyles, E.A.1    Lee, J.C.2
  • 44
    • 0035929295 scopus 로고    scopus 로고
    • Mean DNA bend angle and distribution of DNA bend angles in the CAP-DNA complex in solution
    • Kapanidis A.N., Ebright Y.W., Ludescher R.D., Chan S., and Ebright R.H. Mean DNA bend angle and distribution of DNA bend angles in the CAP-DNA complex in solution. J. Mol. Biol. 312 (2001) 453
    • (2001) J. Mol. Biol. , vol.312 , pp. 453
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ludescher, R.D.3    Chan, S.4    Ebright, R.H.5
  • 45
    • 17944383822 scopus 로고    scopus 로고
    • Elastic rod model of a DNA loop in the lac operon
    • Balaeff A., Mahadevan L., and Schulten K. Elastic rod model of a DNA loop in the lac operon. Phys. Rev. Lett. 83 (1999) 4900
    • (1999) Phys. Rev. Lett. , vol.83 , pp. 4900
    • Balaeff, A.1    Mahadevan, L.2    Schulten, K.3
  • 47
    • 34547852967 scopus 로고    scopus 로고
    • Analysis of in-vivo LacR-mediated gene repression based on the mechanics of DNA looping
    • Zhang Y., McEwen A.E., Crothers D.M., and Levene S.D. Analysis of in-vivo LacR-mediated gene repression based on the mechanics of DNA looping. PLoS ONE 1 (2006) e136
    • (2006) PLoS ONE , vol.1
    • Zhang, Y.1    McEwen, A.E.2    Crothers, D.M.3    Levene, S.D.4
  • 48
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • Seeman N.C., Rosenberg J.M., and Rich A. Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl. Acad. Sci. USA 73 (1976) 804
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 804
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 49
    • 0023461357 scopus 로고
    • Electrostatic calculations and model-building suggest that DNA bound to CAP is sharply bent
    • Warwicker J., Engelman B.P., and Steitz T.A. Electrostatic calculations and model-building suggest that DNA bound to CAP is sharply bent. Proteins 2 (1987) 283
    • (1987) Proteins , vol.2 , pp. 283
    • Warwicker, J.1    Engelman, B.P.2    Steitz, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.