메뉴 건너뛰기




Volumn 94, Issue 9, 2012, Pages 2006-2012

The PWAPA cassette: Intimate association of a PHD-like finger and a winged-helix domain in proteins included in histone-modifying complexes

Author keywords

ATAC; Histone post translational modifications; PcG; Protein domain; Sequence analysis; TrxG

Indexed keywords

HISTONE METHYLTRANSFERASE; POLYCOMB GROUP PROTEIN; POLYCOMB LIKE PROTEIN; UNCLASSIFIED DRUG;

EID: 84864282263     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.05.025     Document Type: Article
Times cited : (6)

References (60)
  • 1
    • 73349092441 scopus 로고    scopus 로고
    • Histones: Annotating chromatin
    • E.I. Campos, and D. Reinberg Histones: annotating chromatin Annu. Rev. Genet. 43 2009 559 599
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 559-599
    • Campos, E.I.1    Reinberg, D.2
  • 2
    • 80052805267 scopus 로고    scopus 로고
    • Histone modification: Cause or cog?
    • S. Henikoff, and A. Shilatifard Histone modification: cause or cog? Trends Genet. 27 2011 389 396
    • (2011) Trends Genet. , vol.27 , pp. 389-396
    • Henikoff, S.1    Shilatifard, A.2
  • 3
    • 75749129110 scopus 로고    scopus 로고
    • PHD fingers: Epigenetic effectors and potential drug targets
    • C.A. Musselman, and T.G. Kutateladze PHD fingers: epigenetic effectors and potential drug targets Mol. Interv. 9 2009 314 323
    • (2009) Mol. Interv. , vol.9 , pp. 314-323
    • Musselman, C.A.1    Kutateladze, T.G.2
  • 4
    • 82255183199 scopus 로고    scopus 로고
    • Handpicking epigenetic marks with PHD fingers
    • C.A. Musselman, and T.G. Kutateladze Handpicking epigenetic marks with PHD fingers Nucleic Acids Res. 39 2011 9061 9071
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9061-9071
    • Musselman, C.A.1    Kutateladze, T.G.2
  • 5
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers
    • DOI 10.1038/nsmb1338, PII NSMB1338
    • S.D. Taverna, H. Li, A.J. Ruthenburg, C.D. Allis, and D.J. Patel How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers Nat. Struct. Mol. Biol. 14 2007 1025 1040 (Pubitemid 350060344)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 6
    • 0031027360 scopus 로고    scopus 로고
    • The human EBNA-2 coactivator p100: Multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development
    • I. Callebaut, and J.-P. Mornon The human EBNA-2 coactivator p100: multidomain organization and relationship to the staphylococcal nuclease fold and to the tudor protein involved in Drosophila melanogaster development Biochem. J. 321 1997 125 132 (Pubitemid 27032578)
    • (1997) Biochemical Journal , vol.321 , Issue.1 , pp. 125-132
    • Callebaut, I.1    Mornon, J.P.2
  • 7
    • 0031081575 scopus 로고    scopus 로고
    • Tudor domains in proteins that interact with RNA
    • DOI 10.1016/S0968-0004(96)30049-2, PII S0968000496300492
    • C.P. Ponting Tudor domains in proteins that interact with RNA Trends Biochem. Sci. 22 1997 51 52 (Pubitemid 27076805)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.2 , pp. 51-52
    • Ponting, C.P.1
  • 11
    • 77951220972 scopus 로고    scopus 로고
    • OST-HTH: A novel predicted RNA-binding domain
    • V. Anantharaman, D. Zhang, and L. Aravind OST-HTH: a novel predicted RNA-binding domain Biol. Direct 5 2010 13
    • (2010) Biol. Direct , vol.5 , pp. 13
    • Anantharaman, V.1    Zhang, D.2    Aravind, L.3
  • 12
    • 77952831715 scopus 로고    scopus 로고
    • LOTUS, a new domain associated with small RNA pathways in the germline
    • I. Callebaut, and J.P. Mornon LOTUS, a new domain associated with small RNA pathways in the germline Bioinformatics 26 2010 1140 1144
    • (2010) Bioinformatics , vol.26 , pp. 1140-1144
    • Callebaut, I.1    Mornon, J.P.2
  • 13
    • 80755169456 scopus 로고    scopus 로고
    • Uniting germline and stem cells: The function of Piwi proteins and the piRNA pathway in diverse organisms
    • C. Juliano, J. Wang, and H. Lin Uniting germline and stem cells: the function of Piwi proteins and the piRNA pathway in diverse organisms Annu. Rev. Genet. 45 2011 447 469
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 447-469
    • Juliano, C.1    Wang, J.2    Lin, H.3
  • 15
    • 44349103099 scopus 로고    scopus 로고
    • A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell
    • DOI 10.1093/nar/gkn146
    • Z. Hong, J. Jiang, L. Lan, S. Nakajima, S. Kanno, H. Koseki, and A. Yasui 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 (Pubitemid 351737186)
    • (2008) Nucleic Acids Research , vol.36 , Issue.9 , pp. 2939-2947
    • Hong, Z.1    Jiang, J.2    Lan, L.3    Nakajima, S.4    Kanno, S.-I.5    Koseki, H.6    Yasui, A.7
  • 16
    • 77954758157 scopus 로고    scopus 로고
    • Polycomb group protein-mediated repression of transcription
    • L. Morey, and K. Helin Polycomb group protein-mediated repression of transcription Trends Biochem. Sci. 35 2010 323 332
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 323-332
    • Morey, L.1    Helin, K.2
  • 18
    • 42149149895 scopus 로고    scopus 로고
    • Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo
    • DOI 10.1128/MCB.02017-07
    • 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 (Pubitemid 351542370)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.8 , pp. 2718-2731
    • Sarma, K.1    Margueron, R.2    Ivanov, A.3    Pirrotta, V.4    Reinberg, D.5
  • 19
    • 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
  • 25
    • 79961027510 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding
    • Y. Chen, B. Wan, K. Wang, F. Cao, Y. Yang, A. Protacio, Y. Dou, H.Y. Chang, and M. Lei Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding EMBO Rep. 12 2011 797 803
    • (2011) EMBO Rep. , vol.12 , pp. 797-803
    • Chen, Y.1    Wan, B.2    Wang, K.3    Cao, F.4    Yang, Y.5    Protacio, A.6    Dou, Y.7    Chang, H.Y.8    Lei, M.9
  • 27
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • I. Letunic, T. Doerks, and P. Bork SMART 7: recent updates to the protein domain annotation resource Nucleic Acids Res. 40 2012 D302 D305
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 31
    • 33846630895 scopus 로고    scopus 로고
    • A generalized analysis of hydrophobic and loop clusters within globular protein sequences
    • R. Eudes, K. Le Tuan, J. Delettre, J.P. Mornon, and I. Callebaut A generalized analysis of hydrophobic and loop clusters within globular protein sequences BMC Struct. Biol. 7 2007 2
    • (2007) BMC Struct. Biol. , vol.7 , pp. 2
    • Eudes, R.1    Le Tuan, K.2    Delettre, J.3    Mornon, J.P.4    Callebaut, I.5
  • 33
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • DOI 10.1093/bib/bbn013, Special Issue: Critical Technologies for Bioinformatics
    • K. Katoh, and H. Toh Recent developments in the MAFFT multiple sequence alignment program Brief Bioinform. 9 2008 286 298 (Pubitemid 351890825)
    • (2008) Briefings in Bioinformatics , vol.9 , Issue.4 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 38
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the universal protein resource (UniProt)
    • UniProt Consortium Reorganizing the protein space at the universal protein resource (UniProt) Nucleic Acids Res. 40 2012 D71 D75
    • (2012) Nucleic Acids Res. , vol.40
    • Consortium, U.1
  • 39
    • 9244265488 scopus 로고    scopus 로고
    • A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers
    • DOI 10.1016/j.gene.2004.09.006, PII S0378111904005505
    • S. Wang, G.P. Roberston, and J. Zhu A novel human homologue of Drosophila polycomblike gene is up-regulated in multiple cancers Gene 343 2004 69 78 (Pubitemid 39551030)
    • (2004) Gene , vol.343 , Issue.1 , pp. 69-78
    • Wang, S.1    Robertson, G.P.2    Zhu, J.3
  • 40
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • DOI 10.1093/emboj/20.24.7137
    • A. Roguev, D. Schaft, A. Shevchenko, W.W. Pijnappel, M. Wilm, R. Aasland, and A.F. Stewart The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4 EMBO J. 20 2001 7137 7148 (Pubitemid 34062305)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.M.P.4    Wilm, M.5    Aasland, R.6    Stewart, A.F.7
  • 42
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • J.R. Horton, A.K. Upadhyay, H.H. Qi, X. Zhang, Y. Shi, and X. Cheng Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases Nat. Struct. Mol. Biol. 17 2010 38 43
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 43
    • 33745818717 scopus 로고    scopus 로고
    • Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
    • DOI 10.1038/nature04814, PII NATURE04814
    • P.V. Peña, F. Davrazou, X. Shi, K.L. Walter, V.V. Verkhusha, O. Gozani, R. Zhao, and T.G. Kutateladze Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2 Nature 442 2006 100 103 (Pubitemid 44064217)
    • (2006) Nature , vol.442 , Issue.7098 , pp. 100-103
    • Pena, P.V.1    Davrazou, F.2    Shi, X.3    Walter, K.L.4    Verkhusha, V.V.5    Gozani, O.6    Zhao, R.7    Kutateladze, T.G.8
  • 45
    • 77953912031 scopus 로고    scopus 로고
    • Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression
    • Z. Wang, J. Song, T.A. Milne, G.G. Wang, H. Li, C.D. Allis, and D.J. Patel Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression Cell 141 2010 1183 1194
    • (2010) Cell , vol.141 , pp. 1183-1194
    • Wang, Z.1    Song, J.2    Milne, T.A.3    Wang, G.G.4    Li, H.5    Allis, C.D.6    Patel, D.J.7
  • 47
    • 77954487796 scopus 로고    scopus 로고
    • Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
    • L. Zeng, Q. Zhang, S. Li, A.N. Plotnikov, M.J. Walsh, and M.M. Zhou Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b Nature 466 2010 258 262
    • (2010) Nature , vol.466 , pp. 258-262
    • Zeng, L.1    Zhang, Q.2    Li, S.3    Plotnikov, A.N.4    Walsh, M.J.5    Zhou, M.M.6
  • 48
    • 34547793043 scopus 로고    scopus 로고
    • Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression
    • DOI 10.1038/nature06034, PII NATURE06034
    • F. Lan, R.E. Collins, R. De Cegli, R. Alpatov, J.R. Horton, X. Shi, O. Gozani, X. Cheng, and Y. Shi Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression Nature 448 2007 718 722 (Pubitemid 47236862)
    • (2007) Nature , vol.448 , Issue.7154 , pp. 718-722
    • Lan, F.1    Collins, R.E.2    De Cegli, R.3    Alpatov, R.4    Horton, J.R.5    Shi, X.6    Gozani, O.7    Cheng, X.8    Shi, Y.9
  • 49
    • 80054709036 scopus 로고    scopus 로고
    • Recognition of unmodified histone H3 by the first PHD finger of Bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases MOZ and MORF
    • S. Qin, L. Jin, J. Zhang, L. Liu, P. Ji, M. Wu, J. Wu, and Y. Shi Recognition of unmodified histone H3 by the first PHD finger of Bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases MOZ and MORF J. Biol. Chem. 286 2011 36944 36955
    • (2011) J. Biol. Chem. , vol.286 , pp. 36944-36955
    • Qin, S.1    Jin, L.2    Zhang, J.3    Liu, L.4    Ji, P.5    Wu, M.6    Wu, J.7    Shi, Y.8
  • 50
    • 79953132180 scopus 로고    scopus 로고
    • Identification of family-determining residues in PHD fingers
    • P. Slama, and D. Geman Identification of family-determining residues in PHD fingers Nucleic Acids Res. 39 2011 1666 1679
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1666-1679
    • Slama, P.1    Geman, D.2
  • 52
    • 77957298474 scopus 로고    scopus 로고
    • Structure of an atypical tudor domain in the Drosophila polycomblike protein
    • A. Friberg, A. Oddone, T. Klymenko, J. Müller, and M. Sattler Structure of an atypical tudor domain in the Drosophila polycomblike protein Protein Sci. 19 2010 1906 1916
    • (2010) Protein Sci. , vol.19 , pp. 1906-1916
    • Friberg, A.1    Oddone, A.2    Klymenko, T.3    Müller, J.4    Sattler, M.5
  • 53
    • 78651240488 scopus 로고    scopus 로고
    • Plant homeodomain fingers form a helping hand for transcription
    • K. Fortschegger, and R. Shiekhattar Plant homeodomain fingers form a helping hand for transcription Epigenetics 6 2011 4 8
    • (2011) Epigenetics , vol.6 , pp. 4-8
    • Fortschegger, K.1    Shiekhattar, R.2
  • 54
    • 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
  • 55
    • 79951500297 scopus 로고    scopus 로고
    • CpG island chromatin: A platform for gene regulation
    • N.P. Blackledge, and R. Klose CpG island chromatin: a platform for gene regulation Epigenetics 6 2011 147 152
    • (2011) Epigenetics , vol.6 , pp. 147-152
    • Blackledge, N.P.1    Klose, R.2
  • 56
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • DOI 10.1038/nature04433, PII NATURE04433
    • Y. Tsukada, J. Fang, H. Erdjument-Bromage, M. Warren, C. Borchers, P. Tempst, and Y. Zhang Histone demethylation by a family of JmjC domain-containing proteins Nature 439 2006 811 816 (Pubitemid 43255695)
    • (2006) Nature , vol.439 , Issue.7078 , pp. 811-816
    • Tsukada, Y.-I.1    Fang, J.2    Erdjument-Bromage, H.3    Warren, M.E.4    Borchers, C.H.5    Tempst, P.6    Zhang, Y.7
  • 57
    • 29244438472 scopus 로고    scopus 로고
    • 4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex
    • DOI 10.1074/jbc.M508312200
    • J.H. Lee, and D.G. Skalnik CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex J. Biol. Chem. 280 2005 41725 41731 (Pubitemid 41832235)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41725-41731
    • Lee, J.-H.1    Skalnik, D.G.2
  • 59


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.