메뉴 건너뛰기




Volumn 57, Issue 2, 2015, Pages 290-303

Molecular basis for SMC rod formation and its dissolution upon DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; COHESIN; CONDENSIN; BACTERIAL DNA; BACTERIAL PROTEIN; CELL CYCLE PROTEIN; PROTEIN BINDING; SMC PROTEIN, BACTERIA;

EID: 84921445757     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.11.023     Document Type: Article
Times cited : (109)

References (41)
  • 1
    • 84871208196 scopus 로고    scopus 로고
    • Self-organization of domain structures by DNA-loop-extruding enzymes
    • Alipour E., Marko J.F. Self-organization of domain structures by DNA-loop-extruding enzymes. Nucleic Acids Res. 2012, 40:11202-11212.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11202-11212
    • Alipour, E.1    Marko, J.F.2
  • 2
    • 0037017393 scopus 로고    scopus 로고
    • Condensin and cohesin display different arm conformations with characteristic hinge angles
    • Anderson D.E., Losada A., Erickson H.P., Hirano T. Condensin and cohesin display different arm conformations with characteristic hinge angles. J.Cell Biol. 2002, 156:419-424.
    • (2002) J.Cell Biol. , vol.156 , pp. 419-424
    • Anderson, D.E.1    Losada, A.2    Erickson, H.P.3    Hirano, T.4
  • 5
    • 2942707858 scopus 로고    scopus 로고
    • DNA interaction and dimerization of eukaryotic SMC hinge domains
    • Chiu A., Revenkova E., Jessberger R. DNA interaction and dimerization of eukaryotic SMC hinge domains. J.Biol. Chem. 2004, 279:26233-26242.
    • (2004) J.Biol. Chem. , vol.279 , pp. 26233-26242
    • Chiu, A.1    Revenkova, E.2    Jessberger, R.3
  • 6
    • 79961029402 scopus 로고    scopus 로고
    • Condensin structures chromosomal DNA through topological links
    • Cuylen S., Metz J., Haering C.H. Condensin structures chromosomal DNA through topological links. Nat. Struct. Mol. Biol. 2011, 18:894-901.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 894-901
    • Cuylen, S.1    Metz, J.2    Haering, C.H.3
  • 7
    • 84857334794 scopus 로고    scopus 로고
    • Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope
    • Fuentes-Perez M.E., Gwynn E.J., Dillingham M.S., Moreno-Herrero F. Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope. Biophys. J. 2012, 102:839-848.
    • (2012) Biophys. J. , vol.102 , pp. 839-848
    • Fuentes-Perez, M.E.1    Gwynn, E.J.2    Dillingham, M.S.3    Moreno-Herrero, F.4
  • 8
    • 78650784720 scopus 로고    scopus 로고
    • Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein hinge domain
    • Griese J.J., Hopfner K.P. Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein hinge domain. Proteins 2011, 79:558-568.
    • (2011) Proteins , vol.79 , pp. 558-568
    • Griese, J.J.1    Hopfner, K.P.2
  • 9
    • 77953574613 scopus 로고    scopus 로고
    • Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins
    • Griese J.J., Witte G., Hopfner K.P. Structure and DNA binding activity of the mouse condensin hinge domain highlight common and diverse features of SMC proteins. Nucleic Acids Res. 2010, 38:3454-3465.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3454-3465
    • Griese, J.J.1    Witte, G.2    Hopfner, K.P.3
  • 11
    • 84895070168 scopus 로고    scopus 로고
    • Interlinked sister chromosomes arise in the absence of condensin during fast replication in B. subtilis
    • Gruber S., Veening J.W., Bach J., Blettinger M., Bramkamp M., Errington J. Interlinked sister chromosomes arise in the absence of condensin during fast replication in B. subtilis. Current biology: CB 2014, 24:293-298.
    • (2014) Current biology: CB , vol.24 , pp. 293-298
    • Gruber, S.1    Veening, J.W.2    Bach, J.3    Blettinger, M.4    Bramkamp, M.5    Errington, J.6
  • 12
    • 0036242551 scopus 로고    scopus 로고
    • Molecular architecture of SMC proteins and the yeast cohesin complex
    • Haering C.H., Löwe J., Hochwagen A., Nasmyth K. Molecular architecture of SMC proteins and the yeast cohesin complex. Mol. Cell 2002, 9:773-788.
    • (2002) Mol. Cell , vol.9 , pp. 773-788
    • Haering, C.H.1    Löwe, J.2    Hochwagen, A.3    Nasmyth, K.4
  • 14
    • 84864752050 scopus 로고    scopus 로고
    • Condensins: universal organizers of chromosomes with diverse functions
    • Hirano T. Condensins: universal organizers of chromosomes with diverse functions. Genes Dev. 2012, 26:1659-1678.
    • (2012) Genes Dev. , vol.26 , pp. 1659-1678
    • Hirano, T.1
  • 15
    • 30744441604 scopus 로고    scopus 로고
    • Opening closed arms: long-distance activation of SMC ATPase by hinge-DNA interactions
    • Hirano M., Hirano T. Opening closed arms: long-distance activation of SMC ATPase by hinge-DNA interactions. Mol. Cell 2006, 21:175-186.
    • (2006) Mol. Cell , vol.21 , pp. 175-186
    • Hirano, M.1    Hirano, T.2
  • 18
    • 0030874421 scopus 로고    scopus 로고
    • ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation
    • Kimura K., Hirano T. ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation. Cell 1997, 90:625-634.
    • (1997) Cell , vol.90 , pp. 625-634
    • Kimura, K.1    Hirano, T.2
  • 19
    • 77951245614 scopus 로고    scopus 로고
    • Crystal structure of the MukB hinge domain with coiled-coil stretches and its functional implications
    • Ku B., Lim J.H., Shin H.C., Shin S.Y., Oh B.H. Crystal structure of the MukB hinge domain with coiled-coil stretches and its functional implications. Proteins 2010, 78:1483-1490.
    • (2010) Proteins , vol.78 , pp. 1483-1490
    • Ku, B.1    Lim, J.H.2    Shin, H.C.3    Shin, S.Y.4    Oh, B.H.5
  • 21
    • 70450225043 scopus 로고    scopus 로고
    • The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB
    • Li Y., Schoeffler A.J., Berger J.M., Oakley M.G. The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB. J.Mol. Biol. 2010, 395:11-19.
    • (2010) J.Mol. Biol. , vol.395 , pp. 11-19
    • Li, Y.1    Schoeffler, A.J.2    Berger, J.M.3    Oakley, M.G.4
  • 22
    • 0037124369 scopus 로고    scopus 로고
    • Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein
    • Mascarenhas J., Soppa J., Strunnikov A.V., Graumann P.L. Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein. EMBO J. 2002, 21:3108-3118.
    • (2002) EMBO J. , vol.21 , pp. 3108-3118
    • Mascarenhas, J.1    Soppa, J.2    Strunnikov, A.V.3    Graumann, P.L.4
  • 23
    • 20744431773 scopus 로고    scopus 로고
    • Comparison of MukB homodimer versus MukBEF complex molecular architectures by electron microscopy reveals a higher-order multimerization
    • Matoba K., Yamazoe M., Mayanagi K., Morikawa K., Hiraga S. Comparison of MukB homodimer versus MukBEF complex molecular architectures by electron microscopy reveals a higher-order multimerization. Biochem. Biophys. Res. Commun. 2005, 333:694-702.
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 694-702
    • Matoba, K.1    Yamazoe, M.2    Mayanagi, K.3    Morikawa, K.4    Hiraga, S.5
  • 24
    • 0032555919 scopus 로고    scopus 로고
    • The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge
    • Melby T.E., Ciampaglio C.N., Briscoe G., Erickson H.P. The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge. J.Cell Biol. 1998, 142:1595-1604.
    • (1998) J.Cell Biol. , vol.142 , pp. 1595-1604
    • Melby, T.E.1    Ciampaglio, C.N.2    Briscoe, G.3    Erickson, H.P.4
  • 25
    • 24944540931 scopus 로고    scopus 로고
    • Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA
    • Moreno-Herrero F., de Jager M., Dekker N.H., Kanaar R., Wyman C., Dekker C. Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA. Nature 2005, 437:440-443.
    • (2005) Nature , vol.437 , pp. 440-443
    • Moreno-Herrero, F.1    de Jager, M.2    Dekker, N.H.3    Kanaar, R.4    Wyman, C.5    Dekker, C.6
  • 26
    • 0035678054 scopus 로고    scopus 로고
    • Disseminating the genome: joining, resolving, and separating sister chromatids during mitosis and meiosis
    • Nasmyth K. Disseminating the genome: joining, resolving, and separating sister chromatids during mitosis and meiosis. Annu. Rev. Genet. 2001, 35:673-745.
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 673-745
    • Nasmyth, K.1
  • 27
    • 80053495083 scopus 로고    scopus 로고
    • Cohesin: a catenase with separate entry and exit gates?
    • Nasmyth K. Cohesin: a catenase with separate entry and exit gates?. Nat. Cell Biol. 2011, 13:1170-1177.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1170-1177
    • Nasmyth, K.1
  • 28
    • 84899902780 scopus 로고    scopus 로고
    • The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes
    • Nolivos S., Sherratt D. The bacterial chromosome: architecture and action of bacterial SMC and SMC-like complexes. FEMS Microbiol. Rev. 2014, 38:380-392.
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 380-392
    • Nolivos, S.1    Sherratt, D.2
  • 30
    • 33847199666 scopus 로고    scopus 로고
    • Reconstitution and subunit geometry of human condensin complexes
    • Onn I., Aono N., Hirano M., Hirano T. Reconstitution and subunit geometry of human condensin complexes. EMBO J. 2007, 26:1024-1034.
    • (2007) EMBO J. , vol.26 , pp. 1024-1034
    • Onn, I.1    Aono, N.2    Hirano, M.3    Hirano, T.4
  • 31
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • Rambo R.P., Tainer J.A. Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering. Curr. Opin. Struct. Biol. 2010, 20:128-137.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 32
    • 84877778935 scopus 로고    scopus 로고
    • Super-resolution in solution X-ray scattering and its applications to structural systems biology
    • Rambo R.P., Tainer J.A. Super-resolution in solution X-ray scattering and its applications to structural systems biology. Annual review of biophysics 2013, 42:415-441.
    • (2013) Annual review of biophysics , vol.42 , pp. 415-441
    • Rambo, R.P.1    Tainer, J.A.2
  • 35
    • 0036049587 scopus 로고    scopus 로고
    • Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB
    • Soppa J., Kobayashi K., Noirot-Gros M.F., Oesterhelt D., Ehrlich S.D., Dervyn E., Ogasawara N., Moriya S. Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB. Mol. Microbiol. 2002, 45:59-71.
    • (2002) Mol. Microbiol. , vol.45 , pp. 59-71
    • Soppa, J.1    Kobayashi, K.2    Noirot-Gros, M.F.3    Oesterhelt, D.4    Ehrlich, S.D.5    Dervyn, E.6    Ogasawara, N.7    Moriya, S.8
  • 36
    • 84870491262 scopus 로고    scopus 로고
    • Condensin, chromatin crossbarring and chromosome condensation
    • Thadani R., Uhlmann F., Heeger S. Condensin, chromatin crossbarring and chromosome condensation. Current biology: CB 2012, 22:R1012-R1021.
    • (2012) Current biology: CB , vol.22 , pp. R1012-R1021
    • Thadani, R.1    Uhlmann, F.2    Heeger, S.3
  • 37
    • 84887822437 scopus 로고    scopus 로고
    • Structural basis for the MukB-topoisomerase IV interaction and its functional implications invivo
    • Vos S.M., Stewart N.K., Oakley M.G., Berger J.M. Structural basis for the MukB-topoisomerase IV interaction and its functional implications invivo. EMBO J. 2013, 32:2950-2962.
    • (2013) EMBO J. , vol.32 , pp. 2950-2962
    • Vos, S.M.1    Stewart, N.K.2    Oakley, M.G.3    Berger, J.M.4
  • 38
    • 0242540364 scopus 로고    scopus 로고
    • A model for ATP hydrolysis-dependent binding of cohesin to DNA
    • Weitzer S., Lehane C., Uhlmann F. A model for ATP hydrolysis-dependent binding of cohesin to DNA. Curr. Biol. 2003, 13:1930-1940.
    • (2003) Curr. Biol. , vol.13 , pp. 1930-1940
    • Weitzer, S.1    Lehane, C.2    Uhlmann, F.3
  • 39
    • 34948899943 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin template
    • Williams R.S., Williams J.S., Tainer J.A. Mre11-Rad50-Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin template. Biochemistry and cell biology 2007, 85:509-520.
    • (2007) Biochemistry and cell biology , vol.85 , pp. 509-520
    • Williams, R.S.1    Williams, J.S.2    Tainer, J.A.3
  • 40
    • 58149152843 scopus 로고    scopus 로고
    • Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions
    • Woo J.S., Lim J.H., Shin H.C., Suh M.K., Ku B., Lee K.H., Joo K., Robinson H., Lee J., Park S.Y., et al. Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions. Cell 2009, 136:85-96.
    • (2009) Cell , vol.136 , pp. 85-96
    • Woo, J.S.1    Lim, J.H.2    Shin, H.C.3    Suh, M.K.4    Ku, B.5    Lee, K.H.6    Joo, K.7    Robinson, H.8    Lee, J.9    Park, S.Y.10
  • 41
    • 0033229882 scopus 로고    scopus 로고
    • Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli
    • Yamazoe M., Onogi T., Sunako Y., Niki H., Yamanaka K., Ichimura T., Hiraga S. Complex formation of MukB, MukE and MukF proteins involved in chromosome partitioning in Escherichia coli. EMBO J. 1999, 18:5873-5884.
    • (1999) EMBO J. , vol.18 , pp. 5873-5884
    • Yamazoe, M.1    Onogi, T.2    Sunako, Y.3    Niki, H.4    Yamanaka, K.5    Ichimura, T.6    Hiraga, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.