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Volumn 387, Issue 1, 2009, Pages 1-9

Binding Kinetics of Histone Chaperone Chz1 and Variant Histone H2A.Z-H2B by Relaxation Dispersion NMR Spectroscopy

Author keywords

binding kinetics; histone chaperone; histone variant; NMR spectroscopy; relaxation dispersion

Indexed keywords

CHAPERONE; CHAPERONE CHZ1; HISTONE H2A; HISTONE H2B; PROTEIN; UNCLASSIFIED DRUG;

EID: 61349122595     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.01.009     Document Type: Article
Times cited : (22)

References (38)
  • 2
    • 44649122151 scopus 로고    scopus 로고
    • Role of histone modifications in defining chromatin structure and function
    • Gelato K.A., and Fischle W. Role of histone modifications in defining chromatin structure and function. Biol. Chem. 389 (2008) 353-363
    • (2008) Biol. Chem. , vol.389 , pp. 353-363
    • Gelato, K.A.1    Fischle, W.2
  • 3
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mäder A.W., Richmond R.K., Sargent D.F., and Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389 (1997) 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • Davey C.A., Sargent D.F., Luger K., Maeder A.W., and Richmond T.J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution. J. Mol. Biol. 319 (2002) 1097-1113
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 6
    • 34249818195 scopus 로고    scopus 로고
    • Histone variants and complexes involved in their exchange
    • Kusch T., and Workman J.L. Histone variants and complexes involved in their exchange. Subcell. Biochem. 41 (2007) 91-109
    • (2007) Subcell. Biochem. , vol.41 , pp. 91-109
    • Kusch, T.1    Workman, J.L.2
  • 7
    • 27144504752 scopus 로고    scopus 로고
    • Histones in functional diversification. Core histone variants
    • Pusarla R.H., and Bhargava P. Histones in functional diversification. Core histone variants. FEBS J. 272 (2005) 5149-5168
    • (2005) FEBS J. , vol.272 , pp. 5149-5168
    • Pusarla, R.H.1    Bhargava, P.2
  • 8
    • 38949091078 scopus 로고    scopus 로고
    • H2A.Z: view from the top
    • Zlatanova J., and Thakar A. H2A.Z: view from the top. Structure 16 (2008) 166-179
    • (2008) Structure , vol.16 , pp. 166-179
    • Zlatanova, J.1    Thakar, A.2
  • 9
    • 0029845086 scopus 로고    scopus 로고
    • H2A.ZI, a new variant histone expressed during Xenopus early development exhibits several distinct features from the core histone H2A
    • Iouzalen N., Moreau J., and Méchali M. H2A.ZI, a new variant histone expressed during Xenopus early development exhibits several distinct features from the core histone H2A. Nucleic Acids Res. 24 (1996) 3947-3952
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3947-3952
    • Iouzalen, N.1    Moreau, J.2    Méchali, M.3
  • 11
    • 0034307468 scopus 로고    scopus 로고
    • Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants
    • Jackson J.D., and Gorovsky M.A. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res. 28 (2000) 3811-3816
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3811-3816
    • Jackson, J.D.1    Gorovsky, M.A.2
  • 12
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • Krogan N.J., Keogh M.C., Datta N., Sawa C., Ryan O.W., Ding H., et al. A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1. Mol. Cell 12 (2003) 1565-1576
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1    Keogh, M.C.2    Datta, N.3    Sawa, C.4    Ryan, O.W.5    Ding, H.6
  • 13
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., et al. A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol. 2 (2004) E131
    • (2004) PLoS Biol. , vol.2
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.L.5    Link, A.J.6
  • 14
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X., Landry J., Wu W.H., Sen S., and Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303 (2004) 343-348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 15
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • Wu W.H., Alami S., Luk E., Wu C.H., Sen S., Mizuguchi G., et al. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat. Struct. Mol. Biol. 12 (2005) 1064-1071
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6
  • 18
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr H.Y., and Purcell E.M. Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys. Rev. 4 (1954) 630-638
    • (1954) Phys. Rev. , vol.4 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 19
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom S., and Gill D. Modified spin-echo method for measuring nuclear relaxation times. Rev. Sci. Instrum. 29 (1958) 688-691
    • (1958) Rev. Sci. Instrum. , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 20
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria J.P., Rance M., and Palmer A.G. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121 (1999) 2331-2332
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 21
    • 0032719427 scopus 로고    scopus 로고
    • A TROSY CPMG sequence for characterizing chemical exchange in large proteins
    • Loria J.P., Rance M., and Palmer A.G. A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15 (1999) 151-155
    • (1999) J. Biomol. NMR , vol.15 , pp. 151-155
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 23
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
    • Millet O., Loria J.P., Kroenke C.D., Pons M., and Palmer A.G. The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 122 (2000) 2867-2877
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer, A.G.5
  • 24
    • 0032871220 scopus 로고    scopus 로고
    • Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution
    • Ishima R., and Torchia D.A. Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J. Biomol. NMR 14 (1999) 369-372
    • (1999) J. Biomol. NMR , vol.14 , pp. 369-372
    • Ishima, R.1    Torchia, D.A.2
  • 25
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5 (1995) 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 26
    • 1242336825 scopus 로고    scopus 로고
    • Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins
    • Orekhov V.Y., Korzhnev D.M., and Kay L.E. Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins. J. Am. Chem. Soc. 126 (2004) 1886-1891
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1886-1891
    • Orekhov, V.Y.1    Korzhnev, D.M.2    Kay, L.E.3
  • 29
    • 33748675500 scopus 로고    scopus 로고
    • Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states
    • Korzhnev D.M., Neudecker P., Zarrine-Afsar A., Davidson A.R., and Kay L.E. Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states. Biochemistry 45 (2006) 10175-10183
    • (2006) Biochemistry , vol.45 , pp. 10175-10183
    • Korzhnev, D.M.1    Neudecker, P.2    Zarrine-Afsar, A.3    Davidson, A.R.4    Kay, L.E.5
  • 30
    • 33846847968 scopus 로고    scopus 로고
    • Prediction of protein-protein association rates from a transition-state theory
    • Alsallaq R., and Zhou H.X. Prediction of protein-protein association rates from a transition-state theory. Structure 15 (2007) 215-224
    • (2007) Structure , vol.15 , pp. 215-224
    • Alsallaq, R.1    Zhou, H.X.2
  • 31
    • 2442640122 scopus 로고    scopus 로고
    • Realistic protein-protein association rates from a simple diffusional model neglecting long-range interactions, free energy barriers, and landscape ruggedness
    • Schlosshauer M., and Baker D. Realistic protein-protein association rates from a simple diffusional model neglecting long-range interactions, free energy barriers, and landscape ruggedness. Protein Sci. 13 (2004) 1660-1669
    • (2004) Protein Sci. , vol.13 , pp. 1660-1669
    • Schlosshauer, M.1    Baker, D.2
  • 32
    • 0141988954 scopus 로고    scopus 로고
    • 15NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin
    • 15NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin. J. Am. Chem. Soc. 125 (2003) 12432-12442
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12432-12442
    • Tolkatchev, D.1    Xu, P.2    Ni, F.3
  • 33
    • 33746220388 scopus 로고    scopus 로고
    • Plug-plug kinetic capillary electrophoresis: method for direct determination of rate constants of complex formation and dissociation
    • Okhonin V., Petrov A.P., Berezovski M., and Krylov S.N. Plug-plug kinetic capillary electrophoresis: method for direct determination of rate constants of complex formation and dissociation. Anal. Chem. 78 (2006) 4803-4810
    • (2006) Anal. Chem. , vol.78 , pp. 4803-4810
    • Okhonin, V.1    Petrov, A.P.2    Berezovski, M.3    Krylov, S.N.4
  • 34
    • 25144459848 scopus 로고    scopus 로고
    • Plasmon light scattering in biology and medicine: new sensing approaches, visions and perspectives
    • Aslan K., Lakowicz J.R., and Geddes C.D. Plasmon light scattering in biology and medicine: new sensing approaches, visions and perspectives. Curr. Opin. Chem. Biol. 9 (2005) 538-544
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 538-544
    • Aslan, K.1    Lakowicz, J.R.2    Geddes, C.D.3
  • 36
    • 39749156063 scopus 로고    scopus 로고
    • Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do?
    • Hansen D.F., Vallurupalli P., Lundström P., Neudecker P., and Kay L.E. Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do?. J. Am. Chem. Soc. 130 (2008) 2667-2675
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2667-2675
    • Hansen, D.F.1    Vallurupalli, P.2    Lundström, P.3    Neudecker, P.4    Kay, L.E.5
  • 37
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell H.M. Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 28 (1958) 430-431
    • (1958) J. Chem. Phys. , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 38
    • 84964203940 scopus 로고
    • Bootstrap methods for standard errors, confidence intervals, and other measures of statistical accuracy
    • Efron B., and Tibshirani R. Bootstrap methods for standard errors, confidence intervals, and other measures of statistical accuracy. Stat. Sci. 1 (1986) 54-77
    • (1986) Stat. Sci. , vol.1 , pp. 54-77
    • Efron, B.1    Tibshirani, R.2


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