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Volumn 40, Issue 21, 2012, Pages 11036-11046

Structure of Actin-related protein 8 and its contribution to nucleosome binding

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN; ACTIN RELATED PROTEIN 4; ACTIN RELATED PROTEIN 8; HISTONE; UNCLASSIFIED DRUG;

EID: 84870595949     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks842     Document Type: Article
Times cited : (44)

References (56)
  • 1
    • 0030754347 scopus 로고    scopus 로고
    • Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family
    • DOI 10.1002/(SICI)1097-0061(19970915)13:11<1053::AID-YEA164>3.0. CO;2-4
    • Poch, O. and Winsor, B. (1997) Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family. Yeast, 13, 1053-1058. (Pubitemid 27368515)
    • (1997) Yeast , vol.13 , Issue.11 , pp. 1053-1058
    • Poch, O.1    Winsor, B.2
  • 2
    • 77954766868 scopus 로고    scopus 로고
    • Actin-related proteins in the nucleus: Life beyond chromatin remodelers
    • Dion, V., Shimada, K. and Gasser, S.M. (2010) Actin-related proteins in the nucleus: life beyond chromatin remodelers. Curr. Opin. Cell Biol., 22, 383-391.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 383-391
    • Dion, V.1    Shimada, K.2    Gasser, S.M.3
  • 3
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • DOI 10.1038/35020123
    • Shen, X., Mizuguchi, G., Hamiche, A. and Wu, C. (2000) A chromatin remodelling complex involved in transcription and DNA processing. Nature, 406, 541-544. (Pubitemid 30625741)
    • (2000) Nature , vol.406 , Issue.6795 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Carl, W.4
  • 4
    • 0348184963 scopus 로고    scopus 로고
    • ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex
    • DOI 10.1126/science.1090701
    • Mizuguchi, G., Shen, X., Landry, J., Wu, W.-H., Sen, S. and Wu, C. (2004) ATP-Driven Exchange of Histone H2AZ Variant Catalyzed by SWR1 Chromatin Remodeling Complex. Science, 303, 343-348. (Pubitemid 38095768)
    • (2004) Science , vol.303 , Issue.5656 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.-H.4    Sen, S.5    Wu, C.6
  • 5
    • 0032508694 scopus 로고    scopus 로고
    • Subunits of the yeast SWI/SNF complex are members of the actin-related protein (ARP) family
    • DOI 10.1074/jbc.273.37.23641
    • Peterson, C.L., Zhao, Y. and Chait, B.T. (1998) Subunits of the yeast SWI/SNF complex are members of the actin-related protein (ARP) Family. J. Biol. Chem., 273, 23641-23644. (Pubitemid 28435690)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 23641-23644
    • Peterson, C.L.1    Zhao, Y.2    Chait, B.T.3
  • 6
    • 0032214123 scopus 로고    scopus 로고
    • Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF
    • Cairns, B.R., Erdjument-Bromage, H., Tempst, P., Winston, F. and Kornberg, R.D. (1998) Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF. Mol. Cell, 2, 639-651. (Pubitemid 128379089)
    • (1998) Molecular Cell , vol.2 , Issue.5 , pp. 639-651
    • Cairns, B.R.1    Erdjument-Bromage, H.2    Tempst, P.3    Winston, F.4    Kornberg, R.D.5
  • 8
    • 0033777258 scopus 로고    scopus 로고
    • Multiple actin-related proteins of Saccharomyces cerevisiae are present in the nucleus
    • Harata, M., Oma, Y., Tabuchi, T., Zhang, Y., Stillman, D.J. and Mizuno, S. (2000) Multiple actin-related proteins of Saccharomyces cerevisiae are present in the nucleus. J. Biochem., 128, 665-671.
    • (2000) J. Biochem. , vol.128 , pp. 665-671
    • Harata, M.1    Oma, Y.2    Tabuchi, T.3    Zhang, Y.4    Stillman, D.J.5    Mizuno, S.6
  • 11
    • 79957907752 scopus 로고    scopus 로고
    • Structural biochemistry of nuclear actinrelated proteins 4 and 8 reveals their interaction with actin
    • Fenn, S., Breitsprecher, D., Gerhold, C.B., Witte, G., Faix, J. and Hopfner, K.-P. (2011) Structural biochemistry of nuclear actinrelated proteins 4 and 8 reveals their interaction with actin. EMBO J., 30, 2153-2166.
    • (2011) EMBO J. , vol.30 , pp. 2153-2166
    • Fenn, S.1    Breitsprecher, D.2    Gerhold, C.B.3    Witte, G.4    Faix, J.5    Hopfner, K.-P.6
  • 12
    • 0042671282 scopus 로고    scopus 로고
    • Involvement of actin-related proteins in ATP-dependent chromatin remodeling
    • DOI 10.1016/S1097-2765(03)00264-8
    • Shen, X., Ranallo, R., Choi, E. and Wu, C. (2003) Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol. Cell, 12, 147-155. (Pubitemid 36945043)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 147-155
    • Shen, X.1    Ranallo, R.2    Choi, E.3    Wu, C.4
  • 13
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • DOI 10.1016/j.cell.2004.11.033, PII S0092867404011018
    • van Attikum, H., Fritsch, O., Hohn, B. and Gasser, S.M. (2004) Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA doublestrand break repair. Cell, 119, 777-788. (Pubitemid 40017685)
    • (2004) Cell , vol.119 , Issue.6 , pp. 777-788
    • Van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 14
    • 34648834736 scopus 로고    scopus 로고
    • Distinct roles for SWR1 and INO80 chromatin remodeling complexes at chromosomal double-strand breaks
    • DOI 10.1038/sj.emboj.7601835, PII 7601835
    • van Attikum, H., Fritsch, O. and Gasser, S.M. (2007) Distinct roles for SWR1 and INO80 chromatin remodeling complexes at chromosomal double-strand breaks. EMBO J., 26, 4113-4125. (Pubitemid 47462094)
    • (2007) EMBO Journal , vol.26 , Issue.18 , pp. 4113-4125
    • Van Attikum, H.1    Fritsch, O.2    Gasser, S.M.3
  • 16
    • 10944267160 scopus 로고    scopus 로고
    • Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites
    • DOI 10.1016/j.molcel.2004.12.003, PII S1097276504007580
    • Downs, J.A., Allard, S., Jobin-Robitaille, O., Javaheri, A., Auger, A., Bouchard, N., Kron, S.J., Jackson, S.P. and Cô té , J. (2004) Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites. Mol. Cell, 16, 979-990. (Pubitemid 40018407)
    • (2004) Molecular Cell , vol.16 , Issue.6 , pp. 979-990
    • Downs, J.A.1    Allard, S.2    Jobin-Robitaille, O.3    Javaheri, A.4    Auger, A.5    Bouchard, N.6    Kron, S.J.7    Jackson, S.P.8    Cote, J.9
  • 17
    • 10944224673 scopus 로고    scopus 로고
    • INO80 and γ-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair
    • DOI 10.1016/j.cell.2004.11.037, PII S0092867404011055
    • Morrison, A.J., Highland, J., Krogan, N.J., Arbel-Eden, A., Greenblatt, J.F., Haber, J.E. and Shen, X. (2004) INO80 and g-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair. Cell, 119, 767-775. (Pubitemid 40017684)
    • (2004) Cell , vol.119 , Issue.6 , pp. 767-775
    • Morrison, A.J.1    Highland, J.2    Krogan, N.J.3    Arbel-Eden, A.4    Greenblatt, J.F.5    Haber, J.E.6    Shen, X.7
  • 19
    • 38949145356 scopus 로고    scopus 로고
    • The actin-related protein hArp8 accumulates on the mitotic chromosomes and functions in chromosome alignment
    • Aoyama, N., Oka, A., Kitayama, K., Kurumizaka, H. and Harata, M. (2008) The actin-related protein hArp8 accumulates on the mitotic chromosomes and functions in chromosome alignment. Exp. Cell Res., 314, 859-868.
    • (2008) Exp. Cell Res. , vol.314 , pp. 859-868
    • Aoyama, N.1    Oka, A.2    Kitayama, K.3    Kurumizaka, H.4    Harata, M.5
  • 20
    • 78651510784 scopus 로고    scopus 로고
    • Global Regulation of H2A.Z Localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity
    • Papamichos-Chronakis, M., Watanabe, S., Rando, O.J. and Peterson, C.L. (2011) Global Regulation of H2A.Z Localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity. Cell, 144, 200-213.
    • (2011) Cell , vol.144 , pp. 200-213
    • Papamichos-Chronakis, M.1    Watanabe, S.2    Rando, O.J.3    Peterson, C.L.4
  • 21
    • 79251545788 scopus 로고    scopus 로고
    • The INO80 ATP-dependent chromatin remodeling complex is a nucleosome spacing factor
    • Udugama, M., Sabri, A. and Bartholomew, B. (2011) The INO80 ATP-dependent chromatin remodeling complex is a nucleosome spacing factor. Mol. Cell. Biol., 31, 662-673.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 662-673
    • Udugama, M.1    Sabri, A.2    Bartholomew, B.3
  • 22
    • 28144462571 scopus 로고    scopus 로고
    • Characterization of a human SWI2/SNF2 like protein hINO80: Demonstration of catalytic and DNA binding activity
    • DOI 10.1016/j.bbrc.2005.10.206, PII S0006291X05024666
    • Bakshi, R., Mehta, A.K., Sharma, R., Maiti, S., Pasha, S. and Brahmachari, V. (2006) Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity. Biochem. Biophys. Res. Commun., 339, 313-320. (Pubitemid 41697551)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.1 , pp. 313-320
    • Bakshi, R.1    Mehta, A.K.2    Sharma, R.3    Maiti, S.4    Pasha, S.5    Brahmachari, V.6
  • 23
    • 33751247668 scopus 로고    scopus 로고
    • Protein complex expression by using multigene baculoviral vectors
    • DOI 10.1038/nmeth983, PII NMETH983
    • Fitzgerald, D.J., Berger, P., Schaffitzel, C., Yamada, K., Richmond, T.J. and Berger, I. (2006) Protein complex expression by using multigene baculoviral vectors. Nat. Meth., 3, 1021-1032. (Pubitemid 44782702)
    • (2006) Nature Methods , vol.3 , Issue.12 , pp. 1021-1032
    • Fitzgerald, D.J.1    Berger, P.2    Schaffitzel, C.3    Yamada, K.4    Richmond, T.J.5    Berger, I.6
  • 24
    • 76449099287 scopus 로고    scopus 로고
    • Xds. Acta crystallogr
    • Kabsch, W. (2010) Xds. Acta Crystallogr. D Biol. Crystallogr., 66, 125-132.
    • (2010) D Biol. Crystallogr. , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 25
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • DOI 10.1107/S0021889808006985, PII S0021889808006985
    • Stein, N. (2008) CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J. Appl. Crystallogr., 41, 641-643. (Pubitemid 351693895)
    • (2008) Journal of Applied Crystallography , vol.41 , Issue.3 , pp. 641-643
    • Stein, N.1
  • 27
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S. and Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protocol, 3, 1171-1179.
    • (2008) Nat. Protocol , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 28
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • DOI 10.1107/S0907444906022116
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. Sect. D, 62, 1002-1011. (Pubitemid 44337374)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.9 , pp. 1002-1011
    • Cowtan, K.1
  • 29
    • 0028103275 scopus 로고
    • The Ccp4 suite programs for protein crystallography
    • Bailey, S. (1994) The Ccp4 suite programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 33
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. (2007) Version 1.2 of the crystallography and NMR system. Nat. Protocol, 2, 2728-2733.
    • (2007) Nat. Protocol , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 36
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam, C.D., Hammel, M., Hura, G.L. and Tainer, J.A. (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Quart. Rev. Biophys., 40, 191-285. (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 38
    • 82555187015 scopus 로고    scopus 로고
    • Oligomerization propensity and flexibility of yeast frataxin studied by X-ray crystallography and small-angle X-ray scattering
    • Söderberg, C.A.G., Shkumatov, A.V., Rajan, S., Gakh, O., Svergun, D.I., Isaya, G. and Al-Karadaghi, S. (2011) Oligomerization propensity and flexibility of yeast frataxin studied by X-ray crystallography and small-angle X-ray scattering. J. Mol. Biol., 414, 783-797.
    • (2011) J. Mol. Biol. , vol.414 , pp. 783-797
    • Söderberg, C.A.G.1    Shkumatov, A.V.2    Rajan, S.3    Gakh, O.4    Svergun, D.I.5    Isaya, G.6    Al-Karadaghi, S.7
  • 39
    • 0035209087 scopus 로고    scopus 로고
    • Using Situs for the registration of protein structures with low-resolution bead models from x-ray solution scattering
    • DOI 10.1107/S0021889801012869
    • Wriggers, W. and Chacon, P. (2001) Using Situs for the registration of protein structures with low-resolution bead models from X-ray solution scattering. J. Appl. Crystallogr., 34, 773-776. (Pubitemid 33144106)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.6 , pp. 773-776
    • Wriggers, W.1    Chacon, P.2
  • 40
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D., Barberato, C. and Koch, M.H.J. (1995) CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 41
    • 58249093392 scopus 로고    scopus 로고
    • Using fluorophore-labeled oligonucleotides to measure affinities of protein-DNA interactions
    • Anderson, B.J., Larkin, C., Guja, K. and Schildbach, J.F. (2008) Using fluorophore-labeled oligonucleotides to measure affinities of protein-DNA interactions. Methods Enzymol., 450, 253-272.
    • (2008) Methods Enzymol. , vol.450 , pp. 253-272
    • Anderson, B.J.1    Larkin, C.2    Guja, K.3    Schildbach, J.F.4
  • 42
    • 84865310327 scopus 로고    scopus 로고
    • Quantifiying chromatin associated interactions: The HI-FI System
    • Winkler, D.D., Luger, K. and Hieb, A.R. (2012) Quantifiying chromatin associated interactions: the HI-FI System. Methods Enzymol., 512, 243-274.
    • (2012) Methods Enzymol. , vol.512 , pp. 243-274
    • Winkler, D.D.1    Luger, K.2    Hieb, A.R.3
  • 45
    • 28644433381 scopus 로고    scopus 로고
    • Sequence and comparative genomic analysis of actin-related proteins
    • DOI 10.1091/mbc.E05-06-0508
    • Muller, J., Oma, Y., Vallar, L., Friederich, E., Poch, O. and Winsor, B. (2005) Sequence and comparative genomic analysis of actin-related proteins. Mol. Biol. Cell., 16, 5736-5748. (Pubitemid 41752222)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5736-5748
    • Muller, J.1    Oma, Y.2    Vallar, L.3    Friederich, E.4    Poch, O.5    Winsor, B.6
  • 46
    • 51049096605 scopus 로고    scopus 로고
    • Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants
    • Iwasa, M., Maeda, K., Narita, A., Maeda, Y. and Oda, T. (2008) Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants. J. Biol. Chem., 283, 21045-21053.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21045-21053
    • Iwasa, M.1    Maeda, K.2    Narita, A.3    Maeda, Y.4    Oda, T.5
  • 47
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii, T., Iwane, A.H., Yanagida, T. and Namba, K. (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature, 467, 724-728.
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 48
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular-to fibrous-actin transition
    • Oda, T., Iwasa, M., Aihara, T., Maeda, Y. and Narita, A. (2009) The nature of the globular-to fibrous-actin transition. Nature, 457, 441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maeda, Y.4    Narita, A.5
  • 49
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin
    • DOI 10.1021/bi011214b
    • Blanchoin, L. and Pollard, T.D. (2001) Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profiliny. Biochemistry, 41, 597-602. (Pubitemid 34062030)
    • (2002) Biochemistry , vol.41 , Issue.2 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 50
    • 0141445972 scopus 로고    scopus 로고
    • Crystal structure of monomeric actin in the ATP state
    • Graceffa, P. and Dominguez, R. (2003) Crystal structure of monomeric actin in the ATP state. J. Biol. Chem., 278, 34172-34180.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34172-34180
    • Graceffa, P.1    Dominguez, R.2
  • 54
    • 84858419821 scopus 로고    scopus 로고
    • Fluorescence strategies for high-throughput quantification of protein interactions
    • Hieb, A.R., D'Arcy, S., Kramer, M.A., White, A.E. and Luger, K. (2012) Fluorescence strategies for high-throughput quantification of protein interactions. Nucleic Acids Res., 40, e33.
    • (2012) Nucleic Acids Res. , vol.40
    • Hieb, A.R.1    D'Arcy, S.2    Kramer, M.A.3    White, A.E.4    Luger, K.5
  • 56
    • 72449167058 scopus 로고    scopus 로고
    • Crystal contacts as nature's docking solutions
    • Krissinel, E. (2010) Crystal contacts as nature's docking solutions. J. Computat. Chem., 31, 133-143.
    • (2010) J. Computat. Chem. , vol.31 , pp. 133-143
    • Krissinel, E.1


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