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Volumn 35, Issue 4, 2016, Pages 376-388

Touch, act and go: Landing and operating on nucleosomes

Author keywords

chromatin; epigenetics; molecular recognition; nucleosome; structural biology

Indexed keywords

DNA; HISTONE; REGULATOR PROTEIN; DNA BINDING PROTEIN; NUCLEAR PROTEIN; NUCLEOSOME;

EID: 84958643027     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201593377     Document Type: Review
Times cited : (19)

References (134)
  • 1
    • 85047671736 scopus 로고    scopus 로고
    • The SANT domain: A putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional corepressor N-CoR and TFIIIB
    • Aasland R, Stewart AF, Gibson T, (1996) The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional corepressor N-CoR and TFIIIB. Trends Biochem Sci 21: 87-88
    • (1996) Trends Biochem Sci , vol.21 , pp. 87-88
    • Aasland, R.1    Stewart, A.F.2    Gibson, T.3
  • 2
    • 84942363868 scopus 로고    scopus 로고
    • Structural insights into nonspecific binding of DNA by TrmBL2, an archaeal chromatin protein
    • Ahmad MU, Waege I, Hausner W, Thomm M, Boos W, Diederichs K, Welte W, (2015) Structural insights into nonspecific binding of DNA by TrmBL2, an archaeal chromatin protein. J Mol Biol 427: 3216-3229
    • (2015) J Mol Biol , vol.427 , pp. 3216-3229
    • Ahmad, M.U.1    Waege, I.2    Hausner, W.3    Thomm, M.4    Boos, W.5    Diederichs, K.6    Welte, W.7
  • 3
    • 84904366454 scopus 로고    scopus 로고
    • Quantitative determination of binding of ISWI to nucleosomes and DNA shows allosteric regulation of DNA binding by nucleotides
    • Al-Ani G, Briggs K, Malik SS, Conner M, Azuma Y, Fischer CJ, (2014a) Quantitative determination of binding of ISWI to nucleosomes and DNA shows allosteric regulation of DNA binding by nucleotides. Biochemistry 53: 4334-4345
    • (2014) Biochemistry , vol.53 , pp. 4334-4345
    • Al-Ani, G.1    Briggs, K.2    Malik, S.S.3    Conner, M.4    Azuma, Y.5    Fischer, C.J.6
  • 6
    • 81555212272 scopus 로고    scopus 로고
    • Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution
    • Armache KJ, Garlick JD, Canzio D, Narlikar GJ, Kingston RE, (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution. Science 334: 977-982
    • (2011) Science , vol.334 , pp. 977-982
    • Armache, K.J.1    Garlick, J.D.2    Canzio, D.3    Narlikar, G.J.4    Kingston, R.E.5
  • 8
    • 84923368907 scopus 로고    scopus 로고
    • How cryo-EM is revolutionizing structural biology
    • Bai XC, McMullan G, Scheres SH, (2015) How cryo-EM is revolutionizing structural biology. Trends Biochem Sci 40: 49-57
    • (2015) Trends Biochem Sci , vol.40 , pp. 49-57
    • Bai, X.C.1    McMullan, G.2    Scheres, S.H.3
  • 10
    • 82455175430 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen, a multifunctional protein central to Kaposi's sarcoma-associated herpesvirus latency
    • Ballestas ME, Kaye KM, (2011) The latency-associated nuclear antigen, a multifunctional protein central to Kaposi's sarcoma-associated herpesvirus latency. Future Microbiol 6: 1399-1413
    • (2011) Future Microbiol , vol.6 , pp. 1399-1413
    • Ballestas, M.E.1    Kaye, K.M.2
  • 11
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister AJ, Kouzarides T, (2011) Regulation of chromatin by histone modifications. Cell Res 21: 381-395
    • (2011) Cell Res , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 13
    • 79551718687 scopus 로고    scopus 로고
    • Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex
    • Baron R, Binda C, Tortorici M, McCammon JA, Mattevi A, (2011) Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex. Structure 19: 212-220
    • (2011) Structure , vol.19 , pp. 212-220
    • Baron, R.1    Binda, C.2    Tortorici, M.3    McCammon, J.A.4    Mattevi, A.5
  • 14
    • 0025291547 scopus 로고
    • The subunit structure of Saccharomyces cerevisiae transcription factor IIIC probed with a novel photocrosslinking reagent
    • Bartholomew B, Kassavetis GA, Braun BR, Geiduschek EP, (1990) The subunit structure of Saccharomyces cerevisiae transcription factor IIIC probed with a novel photocrosslinking reagent. EMBO J 9: 2197-2205
    • (1990) EMBO J , vol.9 , pp. 2197-2205
    • Bartholomew, B.1    Kassavetis, G.A.2    Braun, B.R.3    Geiduschek, E.P.4
  • 15
    • 84902168468 scopus 로고    scopus 로고
    • Regulating the chromatin landscape: Structural and mechanistic perspectives
    • Bartholomew B, (2014) Regulating the chromatin landscape: structural and mechanistic perspectives. Annu Rev Biochem 83: 671-696
    • (2014) Annu Rev Biochem , vol.83 , pp. 671-696
    • Bartholomew, B.1
  • 16
    • 0026419320 scopus 로고
    • Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
    • Bischoff FR, Ponstingl H, (1991) Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature 354: 80-82
    • (1991) Nature , vol.354 , pp. 80-82
    • Bischoff, F.R.1    Ponstingl, H.2
  • 17
    • 84925708107 scopus 로고    scopus 로고
    • Post-translational modifications of histones that influence nucleosome dynamics
    • Bowman GD, Poirier MG, (2015) Post-translational modifications of histones that influence nucleosome dynamics. Chem Rev 115: 2274-2295
    • (2015) Chem Rev , vol.115 , pp. 2274-2295
    • Bowman, G.D.1    Poirier, M.G.2
  • 18
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer LA, Langer MR, Crowley KA, Tan S, Denu JM, Peterson CL, (2002) Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol Cell 10: 935-942
    • (2002) Mol Cell , vol.10 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 19
    • 68249153738 scopus 로고    scopus 로고
    • Silent chromatin at the middle and ends: Lessons from yeasts
    • Buhler M, Gasser SM, (2009) Silent chromatin at the middle and ends: lessons from yeasts. EMBO J 28: 2149-2161
    • (2009) EMBO J , vol.28 , pp. 2149-2161
    • Buhler, M.1    Gasser, S.M.2
  • 20
    • 84863611076 scopus 로고    scopus 로고
    • Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation
    • Campbell SJ, Edwards RA, Leung CC, Neculai D, Hodge CD, Dhe-Paganon S, Glover JN, (2012) Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation. J Biol Chem 287: 23900-23910
    • (2012) J Biol Chem , vol.287 , pp. 23900-23910
    • Campbell, S.J.1    Edwards, R.A.2    Leung, C.C.3    Neculai, D.4    Hodge, C.D.5    Dhe-Paganon, S.6    Glover, J.N.7
  • 22
    • 33845971561 scopus 로고    scopus 로고
    • Characterization of NOBOX DNA binding specificity and its regulation of Gdf9 and Pou5f1 promoters
    • Choi Y, Rajkovic A, (2006) Characterization of NOBOX DNA binding specificity and its regulation of Gdf9 and Pou5f1 promoters. J Biol Chem 281: 35747-35756
    • (2006) J Biol Chem , vol.281 , pp. 35747-35756
    • Choi, Y.1    Rajkovic, A.2
  • 25
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution
    • Davey CA, Sargent DF, Luger K, Maeder AW, Richmond TJ, (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. J Mol Biol 319: 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
  • 26
    • 84928552345 scopus 로고    scopus 로고
    • Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins
    • David Y, Vila-Perello M, Verma S, Muir TW, (2015) Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins. Nat Chem 7: 394-402
    • (2015) Nat Chem , vol.7 , pp. 394-402
    • David, Y.1    Vila-Perello, M.2    Verma, S.3    Muir, T.W.4
  • 27
    • 84857032466 scopus 로고    scopus 로고
    • Structural basis for sequence-specific recognition of DNA by TAL effectors
    • Deng D, Yan C, Pan X, Mahfouz M, Wang J, Zhu JK, Shi Y, Yan N, (2012) Structural basis for sequence-specific recognition of DNA by TAL effectors. Science 335: 720-723
    • (2012) Science , vol.335 , pp. 720-723
    • Deng, D.1    Yan, C.2    Pan, X.3    Mahfouz, M.4    Wang, J.5    Zhu, J.K.6    Shi, Y.7    Yan, N.8
  • 28
    • 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
  • 32
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
    • Falkenberg KJ, Johnstone RW, (2014) Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat Rev Drug Discov 13: 673-691
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 673-691
    • Falkenberg, K.J.1    Johnstone, R.W.2
  • 33
    • 8844281536 scopus 로고    scopus 로고
    • H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding
    • Fan JY, Rangasamy D, Luger K, Tremethick DJ, (2004) H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding. Mol Cell 16: 655-661
    • (2004) Mol Cell , vol.16 , pp. 655-661
    • Fan, J.Y.1    Rangasamy, D.2    Luger, K.3    Tremethick, D.J.4
  • 36
    • 84910082388 scopus 로고    scopus 로고
    • Small molecule control of chromatin remodeling
    • Finley A, Copeland RA, (2014) Small molecule control of chromatin remodeling. Chem Biol 21: 1196-1210
    • (2014) Chem Biol , vol.21 , pp. 1196-1210
    • Finley, A.1    Copeland, R.A.2
  • 37
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle W, Wang Y, Jacobs SA, Kim Y, Allis CD, Khorasanizadeh S, (2003) Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev 17: 1870-1881
    • (2003) Genes Dev , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 38
    • 67649111461 scopus 로고    scopus 로고
    • Use of site-specific protein-DNA photocrosslinking of purified complexes to analyze the topology of the RNA polymerase II transcription initiation complex
    • Forget D, Domecq C, Coulombe B, (2009) Use of site-specific protein-DNA photocrosslinking of purified complexes to analyze the topology of the RNA polymerase II transcription initiation complex. Methods Mol Biol 543: 439-451
    • (2009) Methods Mol Biol , vol.543 , pp. 439-451
    • Forget, D.1    Domecq, C.2    Coulombe, B.3
  • 39
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • Forneris F, Binda C, Vanoni MA, Mattevi A, Battaglioli E, (2005) Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett 579: 2203-2207
    • (2005) FEBS Lett , vol.579 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 40
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris F, Binda C, Adamo A, Battaglioli E, Mattevi A, (2007) Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J Biol Chem 282: 20070-20074
    • (2007) J Biol Chem , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 42
    • 84925397108 scopus 로고    scopus 로고
    • INO80 and SWR complexes: Relating structure to function in chromatin remodeling
    • Gerhold CB, Gasser SM, (2014) INO80 and SWR complexes: relating structure to function in chromatin remodeling. Trends Cell Biol 24: 619-631
    • (2014) Trends Cell Biol , vol.24 , pp. 619-631
    • Gerhold, C.B.1    Gasser, S.M.2
  • 44
    • 84928898379 scopus 로고    scopus 로고
    • Epigenetic modifiers in normal and malignant hematopoiesis
    • Haladyna JN, Yamauchi T, Neff T, Bernt KM, (2015) Epigenetic modifiers in normal and malignant hematopoiesis. Epigenomics 7: 301-320
    • (2015) Epigenomics , vol.7 , pp. 301-320
    • Haladyna, J.N.1    Yamauchi, T.2    Neff, T.3    Bernt, K.M.4
  • 45
    • 84858419821 scopus 로고    scopus 로고
    • Fluorescence strategies for high-throughput quantification of protein interactions
    • Hieb AR, D'Arcy S, Kramer MA, White AE, Luger K, (2012) Fluorescence strategies for high-throughput quantification of protein interactions. Nucleic Acids Res 40: e33
    • (2012) Nucleic Acids Res , vol.40 , pp. e33
    • Hieb, A.R.1    D'Arcy, S.2    Kramer, M.A.3    White, A.E.4    Luger, K.5
  • 46
    • 84555178865 scopus 로고    scopus 로고
    • Mapping protein-DNA and protein-protein interactions of ATP-dependent chromatin remodelers
    • Hota SK, Dechassa ML, Prasad P, Bartholomew B, (2012) Mapping protein-DNA and protein-protein interactions of ATP-dependent chromatin remodelers. Methods Mol Biol 809: 381-409
    • (2012) Methods Mol Biol , vol.809 , pp. 381-409
    • Hota, S.K.1    Dechassa, M.L.2    Prasad, P.3    Bartholomew, B.4
  • 50
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs SA, Khorasanizadeh S, (2002) Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295: 2080-2083
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 51
    • 84936993434 scopus 로고    scopus 로고
    • Histone H3.3 maintains genome integrity during mammalian development
    • Jang CW, Shibata Y, Starmer J, Yee D, Magnuson T, (2015) Histone H3.3 maintains genome integrity during mammalian development. Genes Dev 29: 1377-1392
    • (2015) Genes Dev , vol.29 , pp. 1377-1392
    • Jang, C.W.1    Shibata, Y.2    Starmer, J.3    Yee, D.4    Magnuson, T.5
  • 52
    • 84875502251 scopus 로고    scopus 로고
    • Oxygen, epigenetic signaling, and the evolution of early life
    • Jeltsch A, (2013) Oxygen, epigenetic signaling, and the evolution of early life. Trends Biochem Sci 38: 172-176
    • (2013) Trends Biochem Sci , vol.38 , pp. 172-176
    • Jeltsch, A.1
  • 53
    • 84945186017 scopus 로고    scopus 로고
    • Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2
    • Jiao L, Liu X, (2015) Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2. Science 350: aac4383
    • (2015) Science , vol.350
    • Jiao, L.1    Liu, X.2
  • 54
    • 39749152283 scopus 로고    scopus 로고
    • DNA methyltransferase 3B (DNMT3B) mutations in ICF syndrome lead to altered epigenetic modifications and aberrant expression of genes regulating development, neurogenesis and immune function
    • Jin B, Tao Q, Peng J, Soo HM, Wu W, Ying J, Fields CR, Delmas AL, Liu X, Qiu J, Robertson KD, (2008) DNA methyltransferase 3B (DNMT3B) mutations in ICF syndrome lead to altered epigenetic modifications and aberrant expression of genes regulating development, neurogenesis and immune function. Hum Mol Genet 17: 690-709
    • (2008) Hum Mol Genet , vol.17 , pp. 690-709
    • Jin, B.1    Tao, Q.2    Peng, J.3    Soo, H.M.4    Wu, W.5    Ying, J.6    Fields, C.R.7    Delmas, A.L.8    Liu, X.9    Qiu, J.10    Robertson, K.D.11
  • 55
    • 84875755814 scopus 로고    scopus 로고
    • Influence of metabolism on epigenetics and disease
    • Kaelin WG Jr, McKnight SL, (2013) Influence of metabolism on epigenetics and disease. Cell 153: 56-69
    • (2013) Cell , vol.153 , pp. 56-69
    • Kaelin, W.G.1    McKnight, S.L.2
  • 58
    • 84867906972 scopus 로고    scopus 로고
    • Gatekeepers of chromatin: Small metabolites elicit big changes in gene expression
    • Kaochar S, Tu BP, (2012) Gatekeepers of chromatin: small metabolites elicit big changes in gene expression. Trends Biochem Sci 37: 477-483
    • (2012) Trends Biochem Sci , vol.37 , pp. 477-483
    • Kaochar, S.1    Tu, B.P.2
  • 62
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger H, Armache KJ, Cramer P, (2004) Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol Cell 16: 955-965
    • (2004) Mol Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 63
    • 84931275591 scopus 로고    scopus 로고
    • Extranucleosomal DNA enhances the activity of the LSD1/CoREST histone demethylase complex
    • Kim SA, Chatterjee N, Jennings MJ, Bartholomew B, Tan S, (2015) Extranucleosomal DNA enhances the activity of the LSD1/CoREST histone demethylase complex. Nucleic Acids Res 43: 4868-4880
    • (2015) Nucleic Acids Res , vol.43 , pp. 4868-4880
    • Kim, S.A.1    Chatterjee, N.2    Jennings, M.J.3    Bartholomew, B.4    Tan, S.5
  • 64
    • 84860215207 scopus 로고    scopus 로고
    • Molecular mechanisms and potential functions of histone demethylases
    • Kooistra SM, Helin K, (2012) Molecular mechanisms and potential functions of histone demethylases. Nat Rev Mol Cell Biol 13: 297-311
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 297-311
    • Kooistra, S.M.1    Helin, K.2
  • 65
    • 84897000286 scopus 로고    scopus 로고
    • Biochemistry. The resolution revolution
    • Kuhlbrandt W, (2014) Biochemistry. The resolution revolution. Science 343: 1443-1444
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kuhlbrandt, W.1
  • 68
    • 78650630819 scopus 로고    scopus 로고
    • Fluorescence polarization assays in small molecule screening
    • Lea WA, Simeonov A, (2011) Fluorescence polarization assays in small molecule screening. Expert Opin Drug Discov 6: 17-32
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 17-32
    • Lea, W.A.1    Simeonov, A.2
  • 69
    • 84878039908 scopus 로고    scopus 로고
    • A facile strategy for selective incorporation of phosphoserine into histones
    • Lee S, Oh S, Yang A, Kim J, Soll D, Lee D, Park HS, (2013) A facile strategy for selective incorporation of phosphoserine into histones. Angew Chem Int Ed Engl 52: 5771-5775
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 5771-5775
    • Lee, S.1    Oh, S.2    Yang, A.3    Kim, J.4    Soll, D.5    Lee, D.6    Park, H.S.7
  • 70
    • 84925867973 scopus 로고    scopus 로고
    • Epigenetic mechanisms underlying the link between non-alcoholic fatty liver diseases and nutrition
    • Lee JH, Friso S, Choi SW, (2014) Epigenetic mechanisms underlying the link between non-alcoholic fatty liver diseases and nutrition. Nutrients 6: 3303-3325
    • (2014) Nutrients , vol.6 , pp. 3303-3325
    • Lee, J.H.1    Friso, S.2    Choi, S.W.3
  • 72
    • 77953107054 scopus 로고    scopus 로고
    • The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1
    • Lin Y, Wu Y, Li J, Dong C, Ye X, Chi YI, Evers BM, Zhou BP, (2010) The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1. EMBO J 29: 1803-1816
    • (2010) EMBO J , vol.29 , pp. 1803-1816
    • Lin, Y.1    Wu, Y.2    Li, J.3    Dong, C.4    Ye, X.5    Chi, Y.I.6    Evers, B.M.7    Zhou, B.P.8
  • 73
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ, (1997) Crystal structure of the nucleosome core particle at 2.8 a resolution. Nature 389: 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 75
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration from X-ray structures of its key intermediates
    • Maertens GN, Hare S, Cherepanov P, (2010) The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468: 326-329
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 76
    • 84896725631 scopus 로고    scopus 로고
    • Targeting epigenetics in drug discovery
    • Mai A, (2014) Targeting epigenetics in drug discovery. ChemMedChem 9: 415-417
    • (2014) ChemMedChem , vol.9 , pp. 415-417
    • Mai, A.1
  • 77
    • 77957367439 scopus 로고    scopus 로고
    • Structure of RCC1 chromatin factor bound to the nucleosome core particle
    • Makde RD, England JR, Yennawar HP, Tan S, (2010) Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 467: 562-566
    • (2010) Nature , vol.467 , pp. 562-566
    • Makde, R.D.1    England, J.R.2    Yennawar, H.P.3    Tan, S.4
  • 81
    • 84898725334 scopus 로고    scopus 로고
    • The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A
    • Mattiroli F, Uckelmann M, Sahtoe DD, van Dijk WJ, Sixma TK, (2014) The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A. Nat Commun 5: 3291
    • (2014) Nat Commun , vol.5 , pp. 3291
    • Mattiroli, F.1    Uckelmann, M.2    Sahtoe, D.D.3    Van Dijk, W.J.4    Sixma, T.K.5
  • 82
    • 84946070581 scopus 로고    scopus 로고
    • The right place at the right time: Chaperoning core histone variants
    • Mattiroli F, D'Arcy S, Luger K, (2015) The right place at the right time: chaperoning core histone variants. EMBO Rep 16: 1454-1466
    • (2015) EMBO Rep , vol.16 , pp. 1454-1466
    • Mattiroli, F.1    D'Arcy, S.2    Luger, K.3
  • 84
    • 67650531093 scopus 로고    scopus 로고
    • Determinants of histone H4 N-terminal domain function during nucleosomal array oligomerization: Roles of amino acid sequence, domain length, and charge density
    • McBryant SJ, Klonoski J, Sorensen TC, Norskog SS, Williams S, Resch MG, Toombs JA III, Hobdey SE, Hansen JC, (2009) Determinants of histone H4 N-terminal domain function during nucleosomal array oligomerization: r oles of amino acid sequence, domain length, and charge density. J Biol Chem 284: 16716-16722
    • (2009) J Biol Chem , vol.284 , pp. 16716-16722
    • McBryant, S.J.1    Klonoski, J.2    Sorensen, T.C.3    Norskog, S.S.4    Williams, S.5    Resch, M.G.6    Toombs, J.A.7    Hobdey, S.E.8    Hansen, J.C.9
  • 85
    • 84908408859 scopus 로고    scopus 로고
    • Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome
    • McGinty RK, Henrici RC, Tan S, (2014) Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome. Nature 514: 591-596
    • (2014) Nature , vol.514 , pp. 591-596
    • McGinty, R.K.1    Henrici, R.C.2    Tan, S.3
  • 86
    • 84925743476 scopus 로고    scopus 로고
    • Nucleosome structure and function
    • McGinty RK, Tan S, (2015) Nucleosome structure and function. Chem Rev 115: 2255-2273
    • (2015) Chem Rev , vol.115 , pp. 2255-2273
    • McGinty, R.K.1    Tan, S.2
  • 87
    • 84928533993 scopus 로고    scopus 로고
    • Epigenetic alterations in acute myeloid leukemias
    • Mehdipour P, Santoro F, Minucci S, (2015) Epigenetic alterations in acute myeloid leukemias. FEBS J 282: 1786-1800
    • (2015) FEBS J , vol.282 , pp. 1786-1800
    • Mehdipour, P.1    Santoro, F.2    Minucci, S.3
  • 88
    • 84890835867 scopus 로고    scopus 로고
    • Metabolic mechanisms of epigenetic regulation
    • Meier JL, (2013) Metabolic mechanisms of epigenetic regulation. ACS Chem Biol 8: 2607-2621
    • (2013) ACS Chem Biol , vol.8 , pp. 2607-2621
    • Meier, J.L.1
  • 89
    • 84890176335 scopus 로고    scopus 로고
    • RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
    • Metzger MB, Pruneda JN, Klevit RE, Weissman AM, (2014) RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim Biophys Acta 1843: 47-60
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 47-60
    • Metzger, M.B.1    Pruneda, J.N.2    Klevit, R.E.3    Weissman, A.M.4
  • 90
    • 70350234658 scopus 로고    scopus 로고
    • Dissection of CENP-C-directed centromere and kinetochore assembly
    • Milks KJ, Moree B, Straight AF, (2009) Dissection of CENP-C-directed centromere and kinetochore assembly. Mol Biol Cell 20: 4246-4255
    • (2009) Mol Biol Cell , vol.20 , pp. 4246-4255
    • Milks, K.J.1    Moree, B.2    Straight, A.F.3
  • 91
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
    • Min J, Zhang Y, Xu RM, (2003) Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev 17: 1823-1828
    • (2003) Genes Dev , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 92
    • 34447299689 scopus 로고    scopus 로고
    • Atomic force microscopy imaging of SWI/SNF action: Mapping the nucleosome remodeling and sliding
    • Montel F, Fontaine E, St-Jean P, Castelnovo M, Faivre-Moskalenko C, (2007) Atomic force microscopy imaging of SWI/SNF action: mapping the nucleosome remodeling and sliding. Biophys J 93: 566-578
    • (2007) Biophys J , vol.93 , pp. 566-578
    • Montel, F.1    Fontaine, E.2    St-Jean, P.3    Castelnovo, M.4    Faivre-Moskalenko, C.5
  • 96
    • 69949171492 scopus 로고    scopus 로고
    • On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex
    • Patel A, Dharmarajan V, Vought VE, Cosgrove MS, (2009) On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem 284: 24242-24256
    • (2009) J Biol Chem , vol.284 , pp. 24242-24256
    • Patel, A.1    Dharmarajan, V.2    Vought, V.E.3    Cosgrove, M.S.4
  • 98
    • 67649112269 scopus 로고    scopus 로고
    • Site-directed DNA crosslinking of large multisubunit protein-DNA complexes
    • Persinger J, Bartholomew B, (2009) Site-directed DNA crosslinking of large multisubunit protein-DNA complexes. Methods Mol Biol 543: 453-474
    • (2009) Methods Mol Biol , vol.543 , pp. 453-474
    • Persinger, J.1    Bartholomew, B.2
  • 99
    • 84934439360 scopus 로고    scopus 로고
    • Fluorescent protein specific Nanotraps to study protein-protein interactions and histone-tail peptide binding
    • Pichler G, Leonhardt H, Rothbauer U, (2012) Fluorescent protein specific Nanotraps to study protein-protein interactions and histone-tail peptide binding. Methods Mol Biol 911: 475-483
    • (2012) Methods Mol Biol , vol.911 , pp. 475-483
    • Pichler, G.1    Leonhardt, H.2    Rothbauer, U.3
  • 101
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)
    • Renault L, Kuhlmann J, Henkel A, Wittinghofer A, (2001) Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 105: 245-255
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 104
    • 79952385103 scopus 로고    scopus 로고
    • Analysis of protein-ligand interactions by fluorescence polarization
    • Rossi AM, Taylor CW, (2011) Analysis of protein-ligand interactions by fluorescence polarization. Nat Protoc 6: 365-387
    • (2011) Nat Protoc , vol.6 , pp. 365-387
    • Rossi, A.M.1    Taylor, C.W.2
  • 105
    • 84904541089 scopus 로고    scopus 로고
    • Interpreting the language of histone and DNA modifications
    • Rothbart SB, Strahl BD, (2014) Interpreting the language of histone and DNA modifications. Biochim Biophys Acta 1839: 627-643
    • (2014) Biochim Biophys Acta , vol.1839 , pp. 627-643
    • Rothbart, S.B.1    Strahl, B.D.2
  • 106
    • 84920945391 scopus 로고    scopus 로고
    • Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement
    • Ruan C, Lee CH, Cui H, Li S, Li B, (2015) Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement. Cell Rep 10: 204-215
    • (2015) Cell Rep , vol.10 , pp. 204-215
    • Ruan, C.1    Lee, C.H.2    Cui, H.3    Li, S.4    Li, B.5
  • 108
    • 84908030723 scopus 로고    scopus 로고
    • RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms
    • Ryzhikov M, Gupta R, Glickman M, Korolev S, (2014) RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms. J Biol Chem 289: 28846-28855
    • (2014) J Biol Chem , vol.289 , pp. 28846-28855
    • Ryzhikov, M.1    Gupta, R.2    Glickman, M.3    Korolev, S.4
  • 109
  • 110
    • 34547785073 scopus 로고    scopus 로고
    • Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1
    • Saleque S, Kim J, Rooke HM, Orkin SH, (2007) Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1. Mol Cell 27: 562-572
    • (2007) Mol Cell , vol.27 , pp. 562-572
    • Saleque, S.1    Kim, J.2    Rooke, H.M.3    Orkin, S.H.4
  • 111
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • Schalch T, Duda S, Sargent DF, Richmond TJ, (2005) X-ray structure of a tetranucleosome and its implications for the chromatin fibre. Nature 436: 138-141
    • (2005) Nature , vol.436 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 113
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi YJ, Matson C, Lan F, Iwase S, Baba T, Shi Y, (2005) Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 19: 857-864
    • (2005) Mol Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 114
    • 77950791132 scopus 로고    scopus 로고
    • Installation of site-specific methylation into histones using methyl lysine analogs
    • Chapter 21: Unit 21 18 21-10
    • Simon MD, (2010) Installation of site-specific methylation into histones using methyl lysine analogs. Curr Protoc Mol Biol. Chapter 21: Unit 21 18 21-10
    • (2010) Curr Protoc Mol Biol
    • Simon, M.D.1
  • 115
    • 84899570718 scopus 로고    scopus 로고
    • Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units
    • Song F, Chen P, Sun D, Wang M, Dong L, Liang D, Xu RM, Zhu P, Li G, (2014) Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units. Science 344: 376-380
    • (2014) Science , vol.344 , pp. 376-380
    • Song, F.1    Chen, P.2    Sun, D.3    Wang, M.4    Dong, L.5    Liang, D.6    Xu, R.M.7    Zhu, P.8    Li, G.9
  • 116
    • 58649110597 scopus 로고    scopus 로고
    • Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks
    • Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR, (2009) Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol Cell 33: 181-191
    • (2009) Mol Cell , vol.33 , pp. 181-191
    • Southall, S.M.1    Wong, P.S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 117
    • 84936742306 scopus 로고    scopus 로고
    • BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase
    • Taherbhoy AM, Huang OW, Cochran AG, (2015) BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase. Nat Commun 6: 7621
    • (2015) Nat Commun , vol.6 , pp. 7621
    • Taherbhoy, A.M.1    Huang, O.W.2    Cochran, A.G.3
  • 119
    • 84908151229 scopus 로고    scopus 로고
    • Histone core modifications regulating nucleosome structure and dynamics
    • Tessarz P, Kouzarides T, (2014) Histone core modifications regulating nucleosome structure and dynamics. Nat Rev Mol Cell Biol 15: 703-708
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 703-708
    • Tessarz, P.1    Kouzarides, T.2
  • 120
    • 84902545871 scopus 로고    scopus 로고
    • De novo ANKRD11 and KDM1A gene mutations in a male with features of KBG syndrome and Kabuki syndrome
    • Tunovic S, Barkovich J, Sherr EH, Slavotinek AM, (2014) De novo ANKRD11 and KDM1A gene mutations in a male with features of KBG syndrome and Kabuki syndrome. Am J Med Genet A 164: 1744-1749
    • (2014) Am J Med Genet A , vol.164 , pp. 1744-1749
    • Tunovic, S.1    Barkovich, J.2    Sherr, E.H.3    Slavotinek, A.M.4
  • 121
    • 84931468275 scopus 로고    scopus 로고
    • Disrupted intricacy of histone H3K4 methylation in neurodevelopmental disorders
    • Vallianatos CN, Iwase S, (2015) Disrupted intricacy of histone H3K4 methylation in neurodevelopmental disorders. Epigenomics 7: 503-519
    • (2015) Epigenomics , vol.7 , pp. 503-519
    • Vallianatos, C.N.1    Iwase, S.2
  • 122
    • 77957252758 scopus 로고    scopus 로고
    • Crystal structures of nucleosome core particles containing the '601' strong positioning sequence
    • Vasudevan D, Chua EY, Davey CA, (2010) Crystal structures of nucleosome core particles containing the '601' strong positioning sequence. J Mol Biol 403: 1-10
    • (2010) J Mol Biol , vol.403 , pp. 1-10
    • Vasudevan, D.1    Chua, E.Y.2    Davey, C.A.3
  • 124
    • 84878129207 scopus 로고    scopus 로고
    • Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA
    • Wang F, Li G, Altaf M, Lu C, Currie MA, Johnson A, Moazed D, (2013) Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA. Proc Natl Acad Sci USA 110: 8495-8500
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 8495-8500
    • Wang, F.1    Li, G.2    Altaf, M.3    Lu, C.4    Currie, M.A.5    Johnson, A.6    Moazed, D.7
  • 126
    • 84888862731 scopus 로고    scopus 로고
    • Insm1 controls development of pituitary endocrine cells and requires a SNAG domain for function and for recruitment of histone-modifying factors
    • Welcker JE, Hernandez-Miranda LR, Paul FE, Jia S, Ivanov A, Selbach M, Birchmeier C, (2013) Insm1 controls development of pituitary endocrine cells and requires a SNAG domain for function and for recruitment of histone-modifying factors. Development 140: 4947-4958
    • (2013) Development , vol.140 , pp. 4947-4958
    • Welcker, J.E.1    Hernandez-Miranda, L.R.2    Paul, F.E.3    Jia, S.4    Ivanov, A.5    Selbach, M.6    Birchmeier, C.7
  • 127
    • 84865310327 scopus 로고    scopus 로고
    • Quantifying chromatin-associated interactions: The HI-FI system
    • Winkler DD, Luger K, Hieb AR, (2012) Quantifying 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
  • 128
    • 55249111484 scopus 로고    scopus 로고
    • Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S
    • Xu C, Cui G, Botuyan MV, Mer G, (2008) Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S. Structure 16: 1740-1750
    • (2008) Structure , vol.16 , pp. 1740-1750
    • Xu, C.1    Cui, G.2    Botuyan, M.V.3    Mer, G.4
  • 129
    • 84883744311 scopus 로고    scopus 로고
    • Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain
    • Yang D, Fang Q, Wang M, Ren R, Wang H, He M, Sun Y, Yang N, Xu RM, (2013) Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nat Struct Mol Biol 20: 1116-1118
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 1116-1118
    • Yang, D.1    Fang, Q.2    Wang, M.3    Ren, R.4    Wang, H.5    He, M.6    Sun, Y.7    Yang, N.8    Xu, R.M.9
  • 130
    • 45849115106 scopus 로고    scopus 로고
    • Menin critically links MLL proteins with LEDGF on cancer-associated target genes
    • Yokoyama A, Cleary ML, (2008) Menin critically links MLL proteins with LEDGF on cancer-associated target genes. Cancer Cell 14: 36-46
    • (2008) Cancer Cell , vol.14 , pp. 36-46
    • Yokoyama, A.1    Cleary, M.L.2
  • 131
    • 84862927047 scopus 로고    scopus 로고
    • Reconstitution of modified chromatin templates for in vitro functional assays
    • Yun M, Ruan C, Huh JW, Li B, (2012) Reconstitution of modified chromatin templates for in vitro functional assays. Methods Mol Biol 833: 237-253
    • (2012) Methods Mol Biol , vol.833 , pp. 237-253
    • Yun, M.1    Ruan, C.2    Huh, J.W.3    Li, B.4
  • 132
    • 84873734121 scopus 로고    scopus 로고
    • Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b
    • Zhang Q, Qi S, Xu M, Yu L, Tao Y, Deng Z, Wu W, Li J, Chen Z, Wong J, (2013) Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b. Cell Res 23: 225-241
    • (2013) Cell Res , vol.23 , pp. 225-241
    • Zhang, Q.1    Qi, S.2    Xu, M.3    Yu, L.4    Tao, Y.5    Deng, Z.6    Wu, W.7    Li, J.8    Chen, Z.9    Wong, J.10
  • 133
    • 84900905435 scopus 로고    scopus 로고
    • Microscale thermophoresis for the assessment of nuclear protein-binding affinities
    • Zhang W, Duhr S, Baaske P, Laue E, (2014) Microscale thermophoresis for the assessment of nuclear protein-binding affinities. Methods Mol Biol 1094: 269-276
    • (2014) Methods Mol Biol , vol.1094 , pp. 269-276
    • Zhang, W.1    Duhr, S.2    Baaske, P.3    Laue, E.4
  • 134
    • 84892458543 scopus 로고    scopus 로고
    • A highly conserved region within H2B is important for FACT to act on nucleosomes
    • Zheng S, Crickard JB, Srikanth A, Reese JC, (2014) A highly conserved region within H2B is important for FACT to act on nucleosomes. Mol Cell Biol 34: 303-314
    • (2014) Mol Cell Biol , vol.34 , pp. 303-314
    • Zheng, S.1    Crickard, J.B.2    Srikanth, A.3    Reese, J.C.4


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