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Volumn 19, Issue 2, 2011, Pages 212-220

Molecular mimicry and ligand recognition in binding and catalysis by the histone demethylase LSD1-CoREST complex

Author keywords

[No Author keywords available]

Indexed keywords

COREPRESSOR PROTEIN; HISTONE DEMETHYLASE; HISTONE DEMETHYLASE LSD1; HISTONE DEMETHYLASE LSD2; OXYGEN; PROTEIN COREST; TRANSCRIPTION FACTOR SNAIL; TRANSCRIPTION FACTOR SNAIL1; UNCLASSIFIED DRUG;

EID: 79551718687     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.01.001     Document Type: Article
Times cited : (86)

References (56)
  • 1
    • 77954053278 scopus 로고    scopus 로고
    • LSD1-mediated demethylation of histone H3 lysine 4 triggers Myc-induced transcription
    • S. Amente, A. Bertoni, A. Morano, L. Lania, E.V. Avvedimento, and B. Majello LSD1-mediated demethylation of histone H3 lysine 4 triggers Myc-induced transcription Oncogene 29 2010 3691 3702
    • (2010) Oncogene , vol.29 , pp. 3691-3702
    • Amente, S.1    Bertoni, A.2    Morano, A.3    Lania, L.4    Avvedimento, E.V.5    Majello, B.6
  • 2
    • 0344796204 scopus 로고
    • Ion water interaction potentials derived from free-energy perturbation simulations
    • J. qvist Ion water interaction potentials derived from free-energy perturbation simulations J. Phys. Chem. 94 1990 8021 8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Qvist, J.1
  • 4
    • 70549103613 scopus 로고    scopus 로고
    • The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: Structural biology and biomolecular simulation
    • R. Baron, J.A. McCammon, and A. Mattevi The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: structural biology and biomolecular simulation Curr. Opin. Struct. Biol. 19 2009 672 679
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 672-679
    • Baron, R.1    McCammon, J.A.2    Mattevi, A.3
  • 6
    • 66449098550 scopus 로고    scopus 로고
    • Evolutionary history of the Snail/Scratch superfamily
    • A. Barrallo-Gimeno, and M.A. Nieto Evolutionary history of the Snail/Scratch superfamily Trends Genet. 25 2009 248 252
    • (2009) Trends Genet. , vol.25 , pp. 248-252
    • Barrallo-Gimeno, A.1    Nieto, M.A.2
  • 7
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • H.J.C. Berendsen Interaction models for water in relation to protein hydration B. Pullman, Intermolecular Forces 1981 Riedel Dordrecht, The Nethrelands 331 342
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1
  • 8
    • 34548519907 scopus 로고    scopus 로고
    • A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • DOI 10.1016/S0969-2126(99)80037-9
    • C. Binda, A. Coda, R. Angelini, R. Federico, P. Ascenzi, and A. Mattevi A 30 ngstrom long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase Structure 7 1999 265 276 (Pubitemid 29159686)
    • (1999) Structure , vol.7 , Issue.3 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 9
    • 0037025299 scopus 로고    scopus 로고
    • Structure-function relationships in flavoenzyme-dependent amine oxidations: A comparison of polyamine oxidase and monoamine oxidase
    • DOI 10.1074/jbc.R200005200
    • C. Binda, A. Mattevi, and D.E. Edmondson Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase J. Biol. Chem. 277 2002 23973 23976 (Pubitemid 34951906)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 10
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • D.N. Ciccone, H. Su, S. Hevi, F. Gay, H. Lei, J. Bajko, G. Xu, E. Li, and T. Chen KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints Nature 461 2009 415 418
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6    Xu, G.7    Li, E.8    Chen, T.9
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 15
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • DOI 10.1016/j.febslet.2005.03.015
    • F. Forneris, C. Binda, M. Vanoni, A. Mattevi, and E. Battaglioli Histone demethylation catalyzed by LSD1 is a flavin-dependent oxidative process FEBS Lett. 579 2005 2203 2207 (Pubitemid 40469693)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 17
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • DOI 10.1074/jbc.C700100200
    • F. Forneris, C. Binda, A. Adamo, E. Battaglioli, and A. Mattevi Structural basis of LSD1-CoREST selectivity in histone H3 recognition J. Biol. Chem. 282 2007 20070 20074 (Pubitemid 47099979)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 18
    • 41549132495 scopus 로고    scopus 로고
    • LSD1: Oxidative chemistry for multifaceted functions in chromatin regulation
    • F. Forneris, C. Binda, E. Battaglioli, and A. Mattevi LSD1: oxidative chemistry for multifaceted functions in chromatin regulation Trends Biochem. Sci. 33 2008 181 189
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 181-189
    • Forneris, F.1    Binda, C.2    Battaglioli, E.3    Mattevi, A.4
  • 19
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • B. Hess P-LINCS: a parallel linear constraint solver for molecular simulation J. Chem. Theory Comput. 4 2008 116 122
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 20
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 21
    • 0000424999 scopus 로고
    • Generalization of Noses isothermal molecular-dynamics-non-Hamiltonian dynamics for the canonical ensemble
    • W.G. Hoover Generalization of Noses isothermal molecular-dynamics-non- Hamiltonian dynamics for the canonical ensemble Phys. Rev. A 40 1989 2814 2815
    • (1989) Phys. Rev. A , vol.40 , pp. 2814-2815
    • Hoover, W.G.1
  • 22
    • 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
  • 25
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • T. Jenuwein, and C.D. Allis Translating the histone code Science 293 2001 1074 1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 26
    • 77951698123 scopus 로고    scopus 로고
    • Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase
    • M.S. Jorns, Z.W. Chen, and F.S. Mathews Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase Biochemistry 49 2010 3631 3639
    • (2010) Biochemistry , vol.49 , pp. 3631-3639
    • Jorns, M.S.1    Chen, Z.W.2    Mathews, F.S.3
  • 29
    • 77953107054 scopus 로고    scopus 로고
    • The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1
    • Y. Lin, Y. Wu, J. Li, C. Dong, X. Ye, Y.-I. Chi, B.M. Evers, and B.P. Zhou The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1 EMBO J. 29 2010 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
  • 30
    • 33746309504 scopus 로고    scopus 로고
    • Expression of two insm1-like genes in the developing zebrafish nervous system
    • DOI 10.1016/j.modgep.2005.12.008, PII S1567133X06000032
    • C.M. Lukowski, R.G. Ritzel, and A.J. Waskiewicz Expression of two insm1-like genes in the developing zebrafish nervous system Gene Expr. Patterns 6 2006 711 718 (Pubitemid 44103526)
    • (2006) Gene Expression Patterns , vol.6 , Issue.7 , pp. 711-718
    • Lukowski, C.M.1    Ritzel, R.G.2    Waskiewicz, A.J.3
  • 31
    • 0029057126 scopus 로고
    • Size-independent comparison of protein 3-dimensional structures
    • V.N. Maiorov, and G.M. Crippen Size-independent comparison of protein 3-dimensional structures proteins. 22 1995 273 283
    • (1995) Proteins. , vol.22 , pp. 273-283
    • Maiorov, V.N.1    Crippen, G.M.2
  • 32
    • 33748329757 scopus 로고    scopus 로고
    • The expression of Scratch genes in the developing and adult brain
    • DOI 10.1002/dvdy.20869
    • F. Marín, and M.A. Nieto The expression of Scratch genes in the developing and adult brain Dev. Dyn. 235 2006 2586 2591 (Pubitemid 44325271)
    • (2006) Developmental Dynamics , vol.235 , Issue.9 , pp. 2586-2591
    • Marin, F.1    Nieto, M.A.2
  • 33
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • DOI 10.1016/j.tibs.2006.03.003, PII S0968000406000806
    • A. Mattevi T. be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes Trends Biochem. Sci. 31 2006 276 283 (Pubitemid 43674353)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.5 , pp. 276-283
    • Mattevi, A.1
  • 34
    • 84986440341 scopus 로고
    • Settle: An analytical version of the Shake and Rattle algorithm for rigid water models
    • S. Miyamoto, and P.A. Kollman Settle: an analytical version of the Shake and Rattle algorithm for rigid water models J. Comput. Chem. 13 1992 952 962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 35
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: Biochemical and molecular mechanisms of histone demethylases
    • N. Mosammaparast, and Y. Shi Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases Annu. Rev. Biochem. 79 2010 155 179
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 37
    • 33646076202 scopus 로고    scopus 로고
    • Ovol1 regulates the growth arrest of embryonic epidermal progenitor cells and represses c-myc transcription
    • M. Nair, A. Teng, V. Bilanchone, A. Agrawal, B. Li, and X. Dai Ovol1 regulates the growth arrest of embryonic epidermal progenitor cells and represses c-myc transcription J. Cell Biol. 173 2006 253 264
    • (2006) J. Cell Biol. , vol.173 , pp. 253-264
    • Nair, M.1    Teng, A.2    Bilanchone, V.3    Agrawal, A.4    Li, B.5    Dai, X.6
  • 38
    • 77953121401 scopus 로고    scopus 로고
    • PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity
    • S.S. Nair, B.C. Nair, V. Cortez, D. Chakravarty, E. Metzger, R. Schüle, D.W. Brann, R.R. Tekmal, and R.K. Vadlamudi PELP1 is a reader of histone H3 methylation that facilitates oestrogen receptor-alpha target gene activation by regulating lysine demethylase 1 specificity EMBO Rep. 11 2010 438 444
    • (2010) EMBO Rep. , vol.11 , pp. 438-444
    • Nair, S.S.1    Nair, B.C.2    Cortez, V.3    Chakravarty, D.4    Metzger, E.5    Schüle, R.6    Brann, D.W.7    Tekmal, R.R.8    Vadlamudi, R.K.9
  • 39
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular-dynamics methods
    • S. Nosé A unified formulation of the constant temperature molecular-dynamics methods J. Chem. Phys. 81 1984 511 519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nosé, S.1
  • 40
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • C. Oostenbrink, A. Villa, A.E. Mark, and W.F. van Gunsteren A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 25 2004 1656 1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 41
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals - a new molecular-dynamics method
    • DOI 10.1063/1.328693
    • M. Parrinello, and A. Rahman Polymorphic transitions in single-crystals - a new molecular-dynamics method J. Appl. Phys. 52 1981 7182 7190 (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 43
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • DOI 10.1038/nrm2298, PII NRM2298
    • A.J. Ruthenburg, H. Li, D.J. Patel, and C.D. Allis Multivalent engagement of chromatin modifications by linked binding modules Nat. Rev. Mol. Cell Biol. 8 2007 983 994 (Pubitemid 350174643)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    David Allis, C.4
  • 44
    • 33646940952 scopus 로고
    • Numerical-integration of Cartesian equations of motion of a system with constraints - Molecular-dynamics of N-alkanes
    • J.P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical-integration of Cartesian equations of motion of a system with constraints - molecular-dynamics of N-alkanes J. Comput. Chem. 23 1977 327 341
    • (1977) J. Comput. Chem. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 46
    • 77955288875 scopus 로고    scopus 로고
    • 2-reactivity of flavoproteins: Dynamic access of dioxygen to the active site and role of a H+ relay system in D-amino acid oxidase
    • 2-reactivity of flavoproteins: dynamic access of dioxygen to the active site and role of a H+ relay system in D-amino acid oxidase J. Biol. Chem. 285 2010 24439 24446
    • (2010) J. Biol. Chem. , vol.285 , pp. 24439-24446
    • Saam, J.1    Rosini, E.2    Molla, G.3    Schulten, K.4    Pollegioni, L.5    Ghisla, S.6
  • 47
    • 34547785073 scopus 로고    scopus 로고
    • EpigeEpigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1
    • DOI 10.1016/j.molcel.2007.06.039, PII S1097276507004832
    • S. Saleque, J. Kim, H.M. Rooke, and S.H. Orkin Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1 Mol. Cell 27 2007 562 572 (Pubitemid 47238633)
    • (2007) Molecular Cell , vol.27 , Issue.4 , pp. 562-572
    • Saleque, S.1    Kim, J.2    Rooke, H.M.3    Orkin, S.H.4
  • 48
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Y. Shi, F. Lan, C. Matson, P. Mulligan, J.R. Whetstine, P.A. Cole, R.A. Casero, and Y. Shi Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 Cell 119 2004 941 953 (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 49
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • DOI 10.1038/nature04433, PII NATURE04433
    • Y.-i. Tsukada, J. Fang, H. Erdjument-Bromage, M.E. Warren, C.H. 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
  • 50
    • 77956541159 scopus 로고    scopus 로고
    • A feed-forward circuit controlling inducible NF-κB target gene activation by promoter histone demethylation
    • D. van Essen, Y. Zhu, and S. Saccani A feed-forward circuit controlling inducible NF-κB target gene activation by promoter histone demethylation Mol. Cell 39 2010 750 760
    • (2010) Mol. Cell , vol.39 , pp. 750-760
    • Van Essen, D.1    Zhu, Y.2    Saccani, S.3
  • 51
    • 2142813682 scopus 로고
    • Computer-simulation of molecular-dynamics - Methodology, applications, and perspectives in chemistry
    • W.F. van Gunsteren, and H.J.C. Berendsen Computer-simulation of molecular-dynamics - methodology, applications, and perspectives in chemistry Angew. Chem. Int. Ed. Engl. 29 1990 992 1023
    • (1990) Angew. Chem. Int. Ed. Engl. , vol.29 , pp. 992-1023
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 52
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286 (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 53
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • DOI 10.1016/j.molcel.2006.07.012, PII S1097276506004928
    • M. Yang, C.B. Gocke, X. Luo, D. Borek, D.R. Tomchick, M. Machius, Z. Otwinowski, and H. Yu Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase Mol. Cell 23 2006 377 387 (Pubitemid 44128856)
    • (2006) Molecular Cell , vol.23 , Issue.3 , pp. 377-387
    • Yang, M.1    Gocke, C.B.2    Luo, X.3    Borek, D.4    Tomchick, D.R.5    Machius, M.6    Otwinowski, Z.7    Yu, H.8
  • 55
    • 77949269612 scopus 로고    scopus 로고
    • AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function
    • Z. Yang, J. Jiang, D.M. Stewart, S. Qi, K. Yamane, J. Li, Y. Zhang, and J. Wong AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function Cell Res. 20 2010 276 287
    • (2010) Cell Res. , vol.20 , pp. 276-287
    • Yang, Z.1    Jiang, J.2    Stewart, D.M.3    Qi, S.4    Yamane, K.5    Li, J.6    Zhang, Y.7    Wong, J.8
  • 56
    • 50849101652 scopus 로고    scopus 로고
    • Identification of the oxygen activation site in monomeric sarcosine oxidase: Role of Lys265 in catalysis
    • G. Zhao, R.C. Bruckner, and M.S. Jorns Identification of the oxygen activation site in monomeric sarcosine oxidase: role of Lys265 in catalysis Biochemistry 47 2008 9124 9135
    • (2008) Biochemistry , vol.47 , pp. 9124-9135
    • Zhao, G.1    Bruckner, R.C.2    Jorns, M.S.3


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