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Volumn 23, Issue 19, 2004, Pages 3836-3843

Reaction cycle of the yeast Isw2 chromatin remodeling complex

Author keywords

Chromatin remodeling; Helicase proteins; Isw2

Indexed keywords

FUNGAL PROTEIN; PROTEIN ISW2; UNCLASSIFIED DRUG;

EID: 6344285336     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600364     Document Type: Article
Times cited : (49)

References (42)
  • 1
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker PB, Hörz W (2002) ATP-dependent nucleosome remodeling. Annu Rev Biochem 71: 247-273
    • (2002) Annu Rev Biochem , vol.71 , pp. 247-273
    • Becker, P.B.1    Hörz, W.2
  • 3
    • 18344410319 scopus 로고    scopus 로고
    • dMi-2 and ISWI chromatin remodelling factors have distinct nucleosome binding and mobilization properties
    • Brehm A, Langst G, Kehle J, Clapier CR, Imhof A, Eberharter A, Muller J, Becker PB (2000) dMi-2 and ISWI chromatin remodelling factors have distinct nucleosome binding and mobilization properties. EMBO J 19: 4332-4341
    • (2000) EMBO J , vol.19 , pp. 4332-4341
    • Brehm, A.1    Langst, G.2    Kehle, J.3    Clapier, C.R.4    Imhof, A.5    Eberharter, A.6    Muller, J.7    Becker, P.B.8
  • 4
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER, McKay DB (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA 97: 13080-13085
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 5
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirement for the histone H4 N-terminal tail
    • Dorigo B, Schalch T, Bystricky K, Richmond TJ (2003) Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol 327: 85-96
    • (2003) J Mol Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4
  • 6
    • 0345276461 scopus 로고    scopus 로고
    • Chromatin remodeling in vivo: Evidence for a nucleosome sliding mechanism
    • Fazzio TG, Tsukiyama T (2003) Chromatin remodeling in vivo: evidence for a nucleosome sliding mechanism. Mol Cell 12: 1333-1340
    • (2003) Mol Cell , vol.12 , pp. 1333-1340
    • Fazzio, T.G.1    Tsukiyama, T.2
  • 7
    • 0032103910 scopus 로고    scopus 로고
    • Unique translational positioning of nucleosomes on synthetic DNAs
    • Fitzgerald DJ, Anderson JN (1998) Unique translational positioning of nucleosomes on synthetic DNAs. Nucleic Acids Res 26: 2526-2535
    • (1998) Nucleic Acids Res , vol.26 , pp. 2526-2535
    • Fitzgerald, D.J.1    Anderson, J.N.2
  • 8
    • 0029928550 scopus 로고    scopus 로고
    • Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals
    • Flaus A, Luger K, Tan S, Richmond TJ (1996) Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals. Proc Natl Acad Sci USA 93: 1370-1375
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1370-1375
    • Flaus, A.1    Luger, K.2    Tan, S.3    Richmond, T.J.4
  • 9
    • 0035313855 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling
    • Flaus A, Owen-Hughes T (2001) Mechanisms for ATP-dependent chromatin remodelling. Curr Opin Genet Dev 11: 148-154
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 148-154
    • Flaus, A.1    Owen-Hughes, T.2
  • 10
    • 0037158744 scopus 로고    scopus 로고
    • Dynamics of ATP-dependent chromatin assembly by ACF
    • Fyodorov DV, Kadonaga JT (2002) Dynamics of ATP-dependent chromatin assembly by ACF. Nature 418: 896-900
    • (2002) Nature , vol.418 , pp. 896-900
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 11
    • 0038381469 scopus 로고    scopus 로고
    • Chromatin remodeling activities act on UV-damaged nucleosomes and modulate DNA damage accessibility to photolyase
    • Gaillard H, Fitzgerald DJ, Smith CL, Peterson CL, Richmond TJ, Thoma F (2003) Chromatin remodeling activities act on UV-damaged nucleosomes and modulate DNA damage accessibility to photolyase. J Biol Chem 278: 17655-17663
    • (2003) J Biol Chem , vol.278 , pp. 17655-17663
    • Gaillard, H.1    Fitzgerald, D.J.2    Smith, C.L.3    Peterson, C.L.4    Richmond, T.J.5    Thoma, F.6
  • 12
    • 0035016612 scopus 로고    scopus 로고
    • Interactions of ISW2 chromatin remodeling complex with nucleosomal arrays: Analyses using recombinant yeast histones and immobilized templates
    • Gelbart ME, Rechsteiner T, Richmond TJ, Tsukiyama T (2001) Interactions of ISW2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates. Mol Cell Biol 21: 2098-2106
    • (2001) Mol Cell Biol , vol.21 , pp. 2098-2106
    • Gelbart, M.E.1    Rechsteiner, T.2    Richmond, T.J.3    Tsukiyama, T.4
  • 13
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE, Koonin EV (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3: 419-429
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 14
    • 0037195926 scopus 로고    scopus 로고
    • The RNA helicase DbpA exhibits a markedly different conformation in the ADP-bound state when compared with the ATP- or RNA-bound states
    • Henn A, Shi S-P, Zarivach R, Ben-Zeev E, Sagi I (2002) The RNA helicase DbpA exhibits a markedly different conformation in the ADP-bound state when compared with the ATP- or RNA-bound states. J Biol Chem 277: 46559-46565
    • (2002) J Biol Chem , vol.277 , pp. 46559-46565
    • Henn, A.1    Shi, S.-P.2    Zarivach, R.3    Ben-Zeev, E.4    Sagi, I.5
  • 15
    • 0027373139 scopus 로고
    • Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs
    • Hingorani MM, Patel SS (1993) Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry 32: 12478-12487
    • (1993) Biochemistry , vol.32 , pp. 12478-12487
    • Hingorani, M.M.1    Patel, S.S.2
  • 16
    • 0346363763 scopus 로고    scopus 로고
    • Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae
    • Iida T, Araki H (2004) Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae. Mol Cell Biol 24: 217-227
    • (2004) Mol Cell Biol , vol.24 , pp. 217-227
    • Iida, T.1    Araki, H.2
  • 17
    • 0038100136 scopus 로고    scopus 로고
    • Rad54p is a chromatin remodeling enzyme required for heteroduplex DNA joint formation with chromatin
    • Jaskelioff M, Van Komen S, Krebs JE, Sung P, Peterson CL (2003) Rad54p is a chromatin remodeling enzyme required for heteroduplex DNA joint formation with chromatin. J Biol Chem 278: 9212-9218
    • (2003) J Biol Chem , vol.278 , pp. 9212-9218
    • Jaskelioff, M.1    Van Komen, S.2    Krebs, J.E.3    Sung, P.4    Peterson, C.L.5
  • 18
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD (2001) Translating the histone code. Science 293: 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 19
    • 2942561969 scopus 로고    scopus 로고
    • Topography of the ISW2-nucleosome complex: Insights into nucleosome spacing and chromatin remodeling
    • Kagalwala MN, Glaus BJ, Dang W, Zofall M, Bartholomew B (2004) Topography of the ISW2-nucleosome complex: insights into nucleosome spacing and chromatin remodeling. EMBO J 23: 2092-2104
    • (2004) EMBO J , vol.23 , pp. 2092-2104
    • Kagalwala, M.N.1    Glaus, B.J.2    Dang, W.3    Zofall, M.4    Bartholomew, B.5
  • 20
    • 0036837670 scopus 로고    scopus 로고
    • High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2
    • Kassabov SR, Henry NM, Zofall M, Tsukiyama T, Bartholomew B (2002) High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2. Mol Cell Biol 22: 7524-7534
    • (2002) Mol Cell Biol , vol.22 , pp. 7524-7534
    • Kassabov, S.R.1    Henry, N.M.2    Zofall, M.3    Tsukiyama, T.4    Bartholomew, B.5
  • 21
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6: 89-100
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 22
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G (1997) Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90: 635-647
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 23
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP (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
  • 24
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger K, Rechsteiner TJ, Richmond TJ (1999) Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol Biol 119: 1-16
    • (1999) Methods Mol Biol , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 25
    • 0037418195 scopus 로고    scopus 로고
    • Yeast Rad17/Mec3/Ddc1: A sliding clamp for the DNA damage checkpoint
    • Majka J, Burgers PMJ (2003) Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint. Proc Natl Acad Sci USA 100: 2249-2254
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2249-2254
    • Majka, J.1    Burgers, P.M.J.2
  • 26
    • 0034479416 scopus 로고    scopus 로고
    • Crawling and wiggling on DNA: Structural insights to the mechanism of DNA unwinding by helicases
    • Marians KJ (2000) Crawling and wiggling on DNA: structural insights to the mechanism of DNA unwinding by helicases. Structure 8: R227-R235
    • (2000) Structure , vol.8
    • Marians, K.J.1
  • 27
    • 1642321066 scopus 로고    scopus 로고
    • Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo
    • McConnell AD, Gelbart ME, Tsukiyama T (2004) Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo. Mol Cell Biol 24: 2605-2613
    • (2004) Mol Cell Biol , vol.24 , pp. 2605-2613
    • McConnell, A.D.1    Gelbart, M.E.2    Tsukiyama, T.3
  • 28
    • 0034948011 scopus 로고    scopus 로고
    • DNA and ATP binding activities of the baculovirus DNA helicase P143
    • McDougal VV, Guarino LA (2001) DNA and ATP binding activities of the baculovirus DNA helicase P143. J Virol 75: 7206-7209
    • (2001) J Virol , vol.75 , pp. 7206-7209
    • McDougal, V.V.1    Guarino, L.A.2
  • 29
    • 0022429092 scopus 로고
    • Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors
    • Menetski JP, Kowalczykowski SC (1985) Interaction of recA protein with single-stranded DNA. Quantitative aspects of binding affinity modulation by nucleotide cofactors. J Mol Biol 181: 281-295
    • (1985) J Mol Biol , vol.181 , pp. 281-295
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 30
    • 0037102562 scopus 로고    scopus 로고
    • Chromatin remodeling by RSC involves ATP-dependent DNA translocation
    • Saha A, Wittmeyer J, Cairns BR (2002) Chromatin remodeling by RSC involves ATP-dependent DNA translocation. Genes Dev 16: 2120-2134
    • (2002) Genes Dev , vol.16 , pp. 2120-2134
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 31
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya MR, Guo S, Tabor S, Richardson CC, Ellenberger T (1999) Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell 99: 167-177
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 32
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton MR, Sawaya MR, Ellenberger T, Wigley DB (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101: 589-600
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 33
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas P, Dillingham MS, Wiley P, Webb MR, Wigley DB (2000) Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J 19: 3799-3810
    • (2000) EMBO J , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 34
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story RM, Steitz TA (1992) Structure of the recA protein-ADP complex. Nature 355: 374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 35
    • 0031451329 scopus 로고    scopus 로고
    • Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase
    • Studitsky VM, Kassavetis GA, Geiduschek EP, Felsenfeld G (1997) Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase. Science 278: 1960-1963
    • (1997) Science , vol.278 , pp. 1960-1963
    • Studitsky, V.M.1    Kassavetis, G.A.2    Geiduschek, E.P.3    Felsenfeld, G.4
  • 36
    • 0039837085 scopus 로고    scopus 로고
    • Sequence motifs and free energies of selected natural and non-natural nucleosome positioning DNA sequences
    • Thåström A, Lowary PT, Widlund HR, Cao H, Kubista M, Widom J (1999) Sequence motifs and free energies of selected natural and non-natural nucleosome positioning DNA sequences. J Mol Biol 288: 213-229
    • (1999) J Mol Biol , vol.288 , pp. 213-229
    • Thåström, A.1    Lowary, P.T.2    Widlund, H.R.3    Cao, H.4    Kubista, M.5    Widom, J.6
  • 37
    • 0033558873 scopus 로고    scopus 로고
    • Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae
    • Tsukiyama T, Palmer J, Landel CC, Shiloach J, Wu C (1999) Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae. Genes Dev 13: 686-697
    • (1999) Genes Dev , vol.13 , pp. 686-697
    • Tsukiyama, T.1    Palmer, J.2    Landel, C.C.3    Shiloach, J.4    Wu, C.5
  • 38
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97: 75-84
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 39
    • 0030848285 scopus 로고    scopus 로고
    • Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding
    • Walstrom KM, Dozono JM, von Hippel PH (1997) Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding. Biochemistry 36: 7993-8004
    • (1997) Biochemistry , vol.36 , pp. 7993-8004
    • Walstrom, K.M.1    Dozono, J.M.2    Von Hippel, P.H.3
  • 41
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong I, Lohman TM (1992) Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256: 350-355
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2


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