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Volumn 426, Issue 8, 2014, Pages 1651-1660

The tudor domain of the PHD finger protein 1 is a dual reader of lysine trimethylation at lysine 36 of histone H3 and lysine 27 of histone variant H3t

Author keywords

histone methylation; histone variant; Polycomb regulation; protein protein interaction; reading domain

Indexed keywords

HISTONE H3; LYSINE; PHD FINGER PROTEIN 1; POLYCOMB GROUP PROTEIN; PROTEIN; PROTEIN VARIANT; UNCLASSIFIED DRUG;

EID: 84896997808     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.08.009     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • R. Margueron, and D. Reinberg The Polycomb complex PRC2 and its mark in life Nature 469 2011 343 349
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 3
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • A. Sparmann, and M. van Lohuizen Polycomb silencers control cell fate, development and cancer Nat Rev Cancer 6 2006 846 856
    • (2006) Nat Rev Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    Van Lohuizen, M.2
  • 6
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex
    • R. Cao, and Y. Zhang SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex Mol Cell 15 2004 57 67
    • (2004) Mol Cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 7
    • 0035900741 scopus 로고    scopus 로고
    • Polycomblike PHD fingers mediate conserved interaction with enhancer of zeste protein
    • S. O'Connell, L. Wang, S. Robert, C.A. Jones, R. Saint, and R.S. Jones Polycomblike PHD fingers mediate conserved interaction with enhancer of zeste protein J Biol Chem 276 2001 43065 43073
    • (2001) J Biol Chem , vol.276 , pp. 43065-43073
    • O'Connell, S.1    Wang, L.2    Robert, S.3    Jones, C.A.4    Saint, R.5    Jones, R.S.6
  • 8
    • 42149149895 scopus 로고    scopus 로고
    • Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo
    • K. Sarma, R. Margueron, A. Ivanov, V. Pirrotta, and D. Reinberg Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo Mol Cell Biol 28 2008 2718 2731
    • (2008) Mol Cell Biol , vol.28 , pp. 2718-2731
    • Sarma, K.1    Margueron, R.2    Ivanov, A.3    Pirrotta, V.4    Reinberg, D.5
  • 10
    • 84873417354 scopus 로고    scopus 로고
    • An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targeting
    • L. Cai, S.B. Rothbart, R. Lu, B. Xu, W.Y. Chen, and A. Tripathy et al. An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targeting Mol Cell 49 2013 571 582
    • (2013) Mol Cell , vol.49 , pp. 571-582
    • Cai, L.1    Rothbart, S.B.2    Lu, R.3    Xu, B.4    Chen, W.Y.5    Tripathy, A.6
  • 11
    • 84872347438 scopus 로고    scopus 로고
    • Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3
    • S. Qin, Y. Guo, C. Xu, C. Bian, M. Fu, and S. Gong et al. Tudor domains of the PRC2 components PHF1 and PHF19 selectively bind to histone H3K36me3 Biochem Biophys Res Commun 430 2013 547 553
    • (2013) Biochem Biophys Res Commun , vol.430 , pp. 547-553
    • Qin, S.1    Guo, Y.2    Xu, C.3    Bian, C.4    Fu, M.5    Gong, S.6
  • 12
    • 84865279783 scopus 로고    scopus 로고
    • Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3
    • Y. Zheng, S.M. Sweet, R. Popovic, E. Martinez-Garcia, J.D. Tipton, and P.M. Thomas et al. Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3 Proc Natl Acad Sci U S A 109 2012 13549 13554
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 13549-13554
    • Zheng, Y.1    Sweet, S.M.2    Popovic, R.3    Martinez-Garcia, E.4    Tipton, J.D.5    Thomas, P.M.6
  • 13
    • 79151476637 scopus 로고    scopus 로고
    • Detailed specificity analysis of antibodies binding to modified histone tails with peptide arrays
    • I. Bock, A. Dhayalan, S. Kudithipudi, O. Brandt, P. Rathert, and A. Jeltsch Detailed specificity analysis of antibodies binding to modified histone tails with peptide arrays Epigenetics 6 2011 256 263
    • (2011) Epigenetics , vol.6 , pp. 256-263
    • Bock, I.1    Dhayalan, A.2    Kudithipudi, S.3    Brandt, O.4    Rathert, P.5    Jeltsch, A.6
  • 14
    • 79955995634 scopus 로고    scopus 로고
    • The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9
    • A. Dhayalan, R. Tamas, I. Bock, A. Tattermusch, E. Dimitrova, and S. Kudithipudi et al. The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9 Hum Mol Genet 20 2011 2195 2203
    • (2011) Hum Mol Genet , vol.20 , pp. 2195-2203
    • Dhayalan, A.1    Tamas, R.2    Bock, I.3    Tattermusch, A.4    Dimitrova, E.5    Kudithipudi, S.6
  • 15
    • 77954126183 scopus 로고    scopus 로고
    • Chromatin methylation activity of Dnmt3a and Dnmt3a/3L is guided by interaction of the ADD domain with the histone H3 tail
    • Y. Zhang, R. Jurkowska, S. Soeroes, A. Rajavelu, A. Dhayalan, and I. Bock et al. Chromatin methylation activity of Dnmt3a and Dnmt3a/3L is guided by interaction of the ADD domain with the histone H3 tail Nucleic Acids Res 38 2010 4246 4253
    • (2010) Nucleic Acids Res , vol.38 , pp. 4246-4253
    • Zhang, Y.1    Jurkowska, R.2    Soeroes, S.3    Rajavelu, A.4    Dhayalan, A.5    Bock, I.6
  • 16
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants - Ancient wrap artists of the epigenome
    • P.B. Talbert, and S. Henikoff Histone variants - ancient wrap artists of the epigenome Nat Rev Mol Cell Biol 11 2010 264 275
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 19
    • 33846884410 scopus 로고    scopus 로고
    • Improving gene annotation using peptide mass spectrometry
    • S. Tanner, Z. Shen, J. Ng, L. Florea, R. Guigo, and S.P. Briggs et al. Improving gene annotation using peptide mass spectrometry Genome Res 17 2007 231 239
    • (2007) Genome Res , vol.17 , pp. 231-239
    • Tanner, S.1    Shen, Z.2    Ng, J.3    Florea, L.4    Guigo, R.5    Briggs, S.P.6
  • 20
    • 50349087461 scopus 로고    scopus 로고
    • Specificity of the chromodomain y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs
    • W. Fischle, H. Franz, S.A. Jacobs, C.D. Allis, and S. Khorasanizadeh Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs J Biol Chem 283 2008 19626 19635
    • (2008) J Biol Chem , vol.283 , pp. 19626-19635
    • Fischle, W.1    Franz, H.2    Jacobs, S.A.3    Allis, C.D.4    Khorasanizadeh, S.5
  • 21
    • 77953805624 scopus 로고    scopus 로고
    • Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T
    • H. Tachiwana, W. Kagawa, A. Osakabe, K. Kawaguchi, T. Shiga, and Y. Hayashi-Takanaka et al. Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T Proc Natl Acad Sci U S A 107 2010 10454 10459
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10454-10459
    • Tachiwana, H.1    Kagawa, W.2    Osakabe, A.3    Kawaguchi, K.4    Shiga, T.5    Hayashi-Takanaka, Y.6
  • 23
    • 44349103099 scopus 로고    scopus 로고
    • A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell
    • Z. Hong, J. Jiang, L. Lan, S. Nakajima, S. Kanno, and H. Koseki et al. A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell Nucleic Acids Res 36 2008 2939 2947
    • (2008) Nucleic Acids Res , vol.36 , pp. 2939-2947
    • Hong, Z.1    Jiang, J.2    Lan, L.3    Nakajima, S.4    Kanno, S.5    Koseki, H.6
  • 24
    • 0036134395 scopus 로고    scopus 로고
    • Site-directed mutagenesis by polymerase chain reaction
    • A. Jeltsch, and T. Lanio Site-directed mutagenesis by polymerase chain reaction Methods Mol Biol 182 2002 85 94
    • (2002) Methods Mol Biol , vol.182 , pp. 85-94
    • Jeltsch, A.1    Lanio, T.2
  • 25
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports - Principles and applications
    • R. Frank The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports - principles and applications J Immunol Methods 267 2002 13 26
    • (2002) J Immunol Methods , vol.267 , pp. 13-26
    • Frank, R.1
  • 26
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • M.D. Simon, F. Chu, L.R. Racki, C.C. de la Cruz, A.L. Burlingame, and B. Panning et al. The site-specific installation of methyl-lysine analogs into recombinant histones Cell 128 2007 1003 1012
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1    Chu, F.2    Racki, L.R.3    De La Cruz, C.C.4    Burlingame, A.L.5    Panning, B.6
  • 27
    • 80052140473 scopus 로고    scopus 로고
    • Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails
    • I. Bock, S. Kudithipudi, R. Tamas, G. Kungulovski, A. Dhayalan, and A. Jeltsch Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails BMC Biochem 12 2011 48
    • (2011) BMC Biochem , vol.12 , pp. 48
    • Bock, I.1    Kudithipudi, S.2    Tamas, R.3    Kungulovski, G.4    Dhayalan, A.5    Jeltsch, A.6
  • 28
    • 34250782684 scopus 로고    scopus 로고
    • Extraction, purification and analysis of histones
    • D. Shechter, H.L. Dormann, C.D. Allis, and S.B. Hake Extraction, purification and analysis of histones Nat Protoc 2 2007 1445 1457
    • (2007) Nat Protoc , vol.2 , pp. 1445-1457
    • Shechter, D.1    Dormann, H.L.2    Allis, C.D.3    Hake, S.B.4
  • 29
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • A. Shevchenko, H. Tomas, J. Havlis, J.V. Olsen, and M. Mann In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat Protoc 1 2006 2856 2860
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5


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