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Volumn 473, Issue 12, 2016, Pages 1733-1744

The epigenetic regulator smchd1 contains a functional ghkl-type atpase domain

Author keywords

GHKL ATPase; Hsp90; Smchd1.

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 90; NUCLEAR PROTEIN; PROTEIN HISTIDINE KINASE; PROTEIN MUTL; RADICICOL; RECOMBINANT PROTEIN; STRUCTURAL MAINTENANCE OF CHROMOSOMES FLEXIBLE HINGE DOMAIN CONTAINING 1; UNCLASSIFIED DRUG; CHROMATIN; MACROLIDE; NONHISTONE PROTEIN; SMCHD1 PROTEIN, HUMAN;

EID: 84975132661     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BCJ20160189     Document Type: Article
Times cited : (23)

References (61)
  • 6
    • 84901274317 scopus 로고    scopus 로고
    • Epigenetic characterization of the growth hormone gene identifies SmcHD1 as a regulator of autosomal gene clusters
    • Massah, S., Hollebakken, R., Labrecque, M.P., Kolybaba, A.M., Beischlag, T.V. and Prefontaine, G.G. (2014) Epigenetic characterization of the growth hormone gene identifies SmcHD1 as a regulator of autosomal gene clusters. PLoS One 9, e97535
    • (2014) PLoS One , vol.9 , pp. e97535
    • Massah, S.1    Hollebakken, R.2    Labrecque, M.P.3    Kolybaba, A.M.4    Beischlag, T.V.5    Prefontaine, G.G.6
  • 11
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta, R. and Inouye, M. (2000) GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25, 24-28
    • (2000) Trends Biochem. Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 12
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat, A., de Massy, B., Gadelle, D., Varoutas, P.C., Nicolas, A. and Forterre, P. (1997) An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 386, 414-417
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    De Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5    Forterre, P.6
  • 13
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: Diversity of domain organization
    • Dutta, R., Qin, L. and Inouye, M. (1999) Histidine kinases: diversity of domain organization. Mol. Microbiol. 34, 633-640
    • (1999) Mol. Microbiol , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 14
    • 0030901877 scopus 로고    scopus 로고
    • A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
    • Prodromou, C., Roe, S.M., Piper, P.W. and Pearl, L.H. (1997) A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nat. Struct. Biol. 4, 477-482
    • (1997) Nat. Struct. Biol , vol.4 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4
  • 15
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B., Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W. and Pearl, L.H. (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBOJ.17, 4829-4836
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 16
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger, J.M., Gamblin, S.J., Harrison, S.C. and Wang, J.C. (1996) Structure and mechanism of DNA topoisomerase II. Nature 379, 225-232
    • (1996) Nature , vol.379 , pp. 225-232
    • Berger, J.M.1    Gamblin, S.J.2    Harrison, S.C.3    Wang, J.C.4
  • 17
    • 0034737716 scopus 로고    scopus 로고
    • Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    • Brino, L., Urzhumtsev, A., Mousli, M., Bronner, C., Mitschler, A., Oudet, P. and Moras, D. (2000) Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center. J. Biol. Chem. 275, 9468-9475
    • (2000) J. Biol. Chem. , vol.275 , pp. 9468-9475
    • Brino, L.1    Urzhumtsev, A.2    Mousli, M.3    Bronner, C.4    Mitschler, A.5    Oudet, P.6    Moras, D.7
  • 18
    • 0032514843 scopus 로고    scopus 로고
    • Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis
    • Ban, C. and Yang, W. (1998) Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis. Cell 95, 541-552
    • (1998) Cell , vol.95 , pp. 541-552
    • Ban, C.1    Yang, W.2
  • 19
    • 0033515522 scopus 로고    scopus 로고
    • Transformation of MutL by ATP binding and hydrolysis: A switch in DNA mismatch repair
    • Ban, C., Junop, M. and Yang, W. (1999) Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97, 85-97
    • (1999) Cell , vol.97 , pp. 85-97
    • Ban, C.1    Junop, M.2    Yang, W.3
  • 20
    • 84861527038 scopus 로고    scopus 로고
    • Involvement of a GHKL ATPase in RNA-directed DNA methylation in Arabidopsis thaliana
    • Lorkovic, Z.J., Naumann, U., Matzke, A.J. and Matzke, M. (2012) Involvement of a GHKL ATPase in RNA-directed DNA methylation in Arabidopsis thaliana. Curr. Biol. 22, 933-938
    • (2012) Curr. Biol , vol.22 , pp. 933-938
    • Lorkovic, Z.J.1    Naumann, U.2    Matzke, A.J.3    Matzke, M.4
  • 22
    • 84883258403 scopus 로고    scopus 로고
    • The stochastic silencing phenotype of Arabidopsis morc6 mutants reveals a role in efficient RNA-directed DNA methylation
    • Brabbs, T.R., He, Z., Hogg, K., Kamenski, A., Li, Y., Paszkiewicz, K.H., Moore, K.A., O'Toole, P., Graham, I.A. and Jones, L. (2013) The stochastic silencing phenotype of Arabidopsis morc6 mutants reveals a role in efficient RNA-directed DNA methylation. Plant J. 75, 836-846
    • (2013) Plant J , vol.75 , pp. 836-846
    • Brabbs, T.R.1    He, Z.2    Hogg, K.3    Kamenski, A.4    Li, Y.5    Paszkiewicz, K.H.6    Moore, K.A.7    O'Toole, P.8    Graham, I.A.9    Jones, L.10
  • 24
    • 73349127026 scopus 로고    scopus 로고
    • Cohesin: Its roles and mechanisms
    • Nasmyth, K. and Haering, C.H. (2009) Cohesin: its roles and mechanisms. Annu. Rev. Genet. 43, 525-558
    • (2009) Annu. Rev. Genet , vol.43 , pp. 525-558
    • Nasmyth, K.1    Haering, C.H.2
  • 25
    • 84959377714 scopus 로고    scopus 로고
    • Condensin-based chromosome organization from bacteria to vertebrates
    • Hirano, T. (2016) Condensin-based chromosome organization from bacteria to vertebrates. Cell 164, 847-857
    • (2016) Cell , vol.164 , pp. 847-857
    • Hirano, T.1
  • 26
    • 84958918006 scopus 로고    scopus 로고
    • Resolving complex chromosome structures during meiosis: Versatile deployment of Smc5/6
    • Verver, D.-E., Hwang, G.-H., Jordan, P.-W. and Hamer, G. (2016) Resolving complex chromosome structures during meiosis: versatile deployment of Smc5/6. Chromosoma 125, 15-27
    • (2016) Chromosoma , vol.125 , pp. 15-27
    • Verver, D.-E.1    Hwang, G.-H.2    Jordan, P.-W.3    Hamer, G.4
  • 28
    • 84975166639 scopus 로고    scopus 로고
    • The hinge domain of the epigenetic repressor Smchd1 adopts an unconventional homodimeric configuration
    • Chen, K., Czabotar, P.-E., Blewitt, M.-E. and Murphy, J.-M. (2016) The hinge domain of the epigenetic repressor Smchd1 adopts an unconventional homodimeric configuration. Biochem. J. 473, 733-742
    • (2016) Biochem J. , vol.473 , pp. 733-742
    • Chen, K.1    Czabotar, P.-E.2    Blewitt, M.-E.3    Murphy, J.-M.4
  • 35
    • 0034711265 scopus 로고    scopus 로고
    • Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid
    • Perugini, M.A., Schuck, P. and Howlett, G.J. (2000) Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid. J. Biol. Chem. 275, 36758-36765
    • (2000) J. Biol. Chem. , vol.275 , pp. 36758-36765
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 36
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 37
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck, P., Perugini, M.A., Gonzales, N.R., Howlett, G.J. and Schubert, D. (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J. 82, 1096-1111
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 38
    • 77949357102 scopus 로고    scopus 로고
    • Detection of the ATPase activity of the molecular chaperones Hsp90 and Hsp72 using the TranscreenerTM ADP assay kit
    • Rowlands, M., McAndrew, C., Prodromou, C., Pearl, L., Kalusa, A., Jones, K., Workman, P. and Aherne, W. (2010) Detection of the ATPase activity of the molecular chaperones Hsp90 and Hsp72 using the TranscreenerTM ADP assay kit. J. Biomol. Screen. 15, 279-286
    • (2010) J. Biomol. Screen. , vol.15 , pp. 279-286
    • Rowlands, M.1    McAndrew, C.2    Prodromou, C.3    Pearl, L.4    Kalusa, A.5    Jones, K.6    Workman, P.7    Aherne, W.8
  • 39
    • 84913575123 scopus 로고    scopus 로고
    • Characterization of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms reveals hexameric assemblies with increased thermal stability
    • Keown, J.R. and Pearce, F.G. (2014) Characterization of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms reveals hexameric assemblies with increased thermal stability. Biochem. J. 464, 413-423
    • (2014) Biochem J. , vol.464 , pp. 413-423
    • Keown, J.R.1    Pearce, F.G.2
  • 40
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. Coli Hsp90 and conformation changes upon ADP binding
    • Huai, Q., Wang, H., Liu, Y., Kim, H.Y., Toft, D. and Ke, H. (2005) Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13, 579-590
    • (2005) Structure , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.Y.4    Toft, D.5    Ke, H.6
  • 42
    • 84863811420 scopus 로고    scopus 로고
    • The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis
    • Cunningham, C.N., Southworth, D.R., Krukenberg, K.A. and Agard, D.A. (2012) The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Sci. 21, 1162-1171
    • (2012) Protein Sci. , vol.21 , pp. 1162-1171
    • Cunningham, C.N.1    Southworth, D.R.2    Krukenberg, K.A.3    Agard, D.A.4
  • 43
    • 0034602451 scopus 로고    scopus 로고
    • C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle
    • Weikl, T., Muschler, P., Richter, K., Veit, T., Reinstein, J. and Buchner, J. (2000) C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle. J. Mol. Biol. 303, 583-592
    • (2000) J. Mol. Biol. , vol.303 , pp. 583-592
    • Weikl, T.1    Muschler, P.2    Richter, K.3    Veit, T.4    Reinstein, J.5    Buchner, J.6
  • 45
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S.M., Panaretou, B., Piper, P.W. and Pearl, L.H. (2003) Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 11, 647-658
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 46
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris, S.F., Shiau, A.K. and Agard, D.A. (2004) The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12, 1087-1097
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 47
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle, P., Siepmann, M., Harst, A., Siderius, M., Reusch, H.P. and Obermann, W.M. (2006) The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell Biol. 26, 8385-8395
    • (2006) Mol. Cell Biol , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, H.P.5    Obermann, W.M.6
  • 49
    • 84874684844 scopus 로고    scopus 로고
    • Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains
    • Wang, C., Sang, J., Wang, J., Su, M., Downey, J.S., Wu, Q., Wang, S., Cai, Y., Xu, X., Wu, J. et al. (2013) Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains. PLoS Biol. 11, e1001493
    • (2013) PLoS Biol , vol.11 , pp. e1001493
    • Wang, C.1    Sang, J.2    Wang, J.3    Su, M.4    Downey, J.S.5    Wu, Q.6    Wang, S.7    Cai, Y.8    Xu, X.9    Wu, J.10
  • 51
    • 0035477839 scopus 로고    scopus 로고
    • Structure and function of the N-terminal 40 kDa fragment of human PMS2: A monomeric GHL ATPase
    • Guarne, A., Junop, M.S. and Yang, W. (2001) Structure and function of the N-terminal 40 kDa fragment of human PMS2: a monomeric GHL ATPase. EMBO J. 20, 5521-5531
    • (2001) EMBO J , vol.20 , pp. 5521-5531
    • Guarne, A.1    Junop, M.S.2    Yang, W.3
  • 52
    • 84939977299 scopus 로고    scopus 로고
    • Small-angle X-ray scattering analysis reveals the ATP-bound monomeric state of the ATPase domain from the homodimeric MutL endonuclease, a GHKL phosphotransferase superfamily protein
    • Iino, H., Hikima, T., Nishida, Y., Yamamoto, M., Kuramitsu, S. and Fukui, K. (2015) Small-angle X-ray scattering analysis reveals the ATP-bound monomeric state of the ATPase domain from the homodimeric MutL endonuclease, a GHKL phosphotransferase superfamily protein. Extremophiles 19, 643-656
    • (2015) Extremophiles , vol.19 , pp. 643-656
    • Iino, H.1    Hikima, T.2    Nishida, Y.3    Yamamoto, M.4    Kuramitsu, S.5    Fukui, K.6
  • 53
    • 0035823582 scopus 로고    scopus 로고
    • Coordinated ATP hydrolysis by the Hsp90 dimer
    • Richter, K., Muschler, P., Hainzl, O. and Buchner, J. (2001) Coordinated ATP hydrolysis by the Hsp90 dimer. J.Biol. Chem. 276, 33689-33696
    • (2001) J. Biol. Chem , vol.276 , pp. 33689-33696
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Buchner, J.4
  • 54
    • 57649215437 scopus 로고    scopus 로고
    • A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s
    • Vaughan, C.K., Piper, P.W., Pearl, L.H. and Prodromou, C. (2009) A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J. 276, 199-209
    • (2009) FEBS J , vol.276 , pp. 199-209
    • Vaughan, C.K.1    Piper, P.W.2    Pearl, L.H.3    Prodromou, C.4
  • 55
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe, S.M., Prodromou, C., O'Brien, R., Ladbury, J.E., Piper, P.W. and Pearl, L.H. (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 57
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 58
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert,X. Gouet,P.2014Deciphering key features in protein structures with the new ENDscript serverNucleic Acids Res.42W320-W324
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 59
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D.I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 60
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M.B. and Svergun, D.I. (2001) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 61
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • 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
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3


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