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The progress in exploring the structure and

  • School of Life Science, University of Science and Technology of China, Hefei 230027, China

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  • Corresponding author: ZANG Jian-ye, E-mail: zangjy@ustc.edu.cn
  • Received Date: 28 June 2008
  • Rev Recd Date: 05 July 2008
  • Publish Date: 31 August 2008
    Abstract

  • Abstract

    The discovery of histone demethylase LSD1 is an important progress in the field of epigenetics, indicating that histone lysine methylation is a reversible and dynamic process like other covalent histone modifications such as acetylation, phosphorylation and ubiquitylation.Structural and functional research results demonstrate that LSD1 regulates the activation and silencing of gene transcription and the function of p53. LSD1 plays a significant role in the development of several cancers and is a potential target protein for developing anti-cancer drugs.

    Abstract

    The discovery of histone demethylase LSD1 is an important progress in the field of epigenetics, indicating that histone lysine methylation is a reversible and dynamic process like other covalent histone modifications such as acetylation, phosphorylation and ubiquitylation.Structural and functional research results demonstrate that LSD1 regulates the activation and silencing of gene transcription and the function of p53. LSD1 plays a significant role in the development of several cancers and is a potential target protein for developing anti-cancer drugs.
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    [1]
    Kornberg R D, Lorch Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome[J]. Cell,1999,98:285-294.
    [2]
    Martin C, Zhang Y. The diverse functions of histone lysine methylation[J]. Nat Rev Mol Cell Biol,2005,6:838-849.
    [3]
    Mailand N, Bekker-Jensen S, Faustrup H, et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins[J]. Cell, 2007,131:887-900.
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    Wyce A, Xiao T, Whelan K A, et al. H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex[J]. Mol Cell,2007,27:275-288.
    [7]
    Volkel P, Angrand P O. The control of histone lysine methylation in epigenetic regulation[J]. Biochimie,2007,89:1-20.
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    Jenuwein T, Allis C D. Translating the histone code[J]. Science,2001,293:1 074-1 080.
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    Ruthenburg A J, Li H, Patel D J, et al. Multivalent engagement of chromatin modifications by linked binding modules[J]. Nat Rev Mol Cell Biol, 2007,8:983-994.
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    Wysocka J, Allis C D, Coonrod S. Histone arginine methylation and its dynamic regulation[J]. Front Biosci, 2006,11:344-355.
    [11]
    Lachner M, OSullivan R J, Jenuwein T. An epigenetic road map for histone lysine methylation[J]. J Cell Sci, 2003,116:2 117-2 124.
    [12]
    Margueron R, Trojer P, Reinberg D. The key to development: Interpreting the histone code[J]. Curr Opin Genet Dev, 2005,15:163-176.
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    Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails[J]. Genes Dev,2001,15:2 343-2 360.
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    Santos-Rosa H, Schneider R, Bannister A J, et al. Active genes are tri-methylated at K4 of histone H3[J]. Nature, 2002.419:407-411.
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    Wysocka J, Swigut T, Xiao H, et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling[J]. Nature, 2006,442:86-90.
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    Shi X, Hong T, Walter K L, et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression[J]. Nature, 2006,442:96-99.
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    Rea S, Eisenhaber F, OCarroll D, et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases[J]. Nature,2000,406:593-599.
    [18]
    Biel M, Wascholowski V, Giannis A. Epigenetics: An epicenter of gene regulation — histones and histone-modifying enzymes[J]. Angew Chem Int Ed Engl, 2005,44:3 186-3 216.
    [19]
    Shahbazian M D, Grunstein M. Functions of site-specific histone acetylation and deacetylation[J]. Annu Rev Biochem,2007,76:75-100.
    [20]
    Zhang Y. Transcriptional regulation by histone ubiquitination and deubiquitination[J]. Genes Dev, 2003,17:2 733-2 740.
    [21]
    Paik W K, Kim S. Enzymatic demethylation of calf thymus histones[J]. Biochem Biophys Res Commun,1973,51:781-788.
    [22]
    Shi Y, Lan F, Matson C, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1[J]. Cell, 2004,119:941-953.
    [23]
    Shi Y, Whetstine J R. Dynamic regulation of histone lysine methylation by demethylases[J]. Mol Cell,2007,25:1-14.
    [24]
    Klose R J, Zhang Y. Regulation of histone methylation by demethylimination and demethylation[J]. Nat Rev Mol Cell Biol, 2007,8:307-318.
    [25]
    Tong J K, Hassig C A, Schnitzler G R, et al. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex[J]. Nature, 1998,395:917-921.
    [26]
    Hakimi M A, Dong Y, Lane W S, et al. A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes[J]. J Biol Chem,2003,278:7 234-7 239.
    [27]
    You A, Tong J K, Grozinger C M, et al. CoREST is an integral component of the CoREST- human histone deacetylase complex[J]. Proc Natl Acad Sci U S A,2001,98:1 454-1 458.
    [28]
    Humphrey G W, Wang Y, Russanova V R, et al. Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1[J]. J Biol Chem, 2001,276:6 817-6 824.
    [29]
    Shi Y, Sawada J, Sui G, et al. Coordinated histone modifications mediated by a CtBP co-repressor complex[J]. Nature, 2003,422:735-738.
    [30]
    Aravind L, Iyer L M. The SWIRM domain: A conserved module found in chromosomal proteins points to novel chromatin-modifying activities[J]. Genome Biol 3, 2002,RESEARCH0039.
    [31]
    Trewick S C, Henshaw T F, Hausinger R P, et al. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage[J]. Nature,2002,419:174-178.
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    Tsukada Y I, Fang J, Erdjument-Bromage H, et al. Histone demethylation by a family of JmjC domain-containing proteins[J]. Nature,2005.
    [33]
    Fang J, Hogan G J, Liang G, et al. The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36Me2[J]. Mol Cell Biol, 2007,27:5 055-5 065.
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    Tu S, Bulloch E M, Yang L, et al. Identification of histone demethylases in Saccharomyces cerevisiae[J]. J Biol Chem, 2007,282:14 262-14 271.
    [35]
    Yamane K, Toumazou C, Tsukada Y, et al. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor[J]. Cell, 2006,125:483-495.
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    Whetstine J R, Nottke A, Lan F, et al. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases[J]. Cell, 2006,125:467-481.
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    Lee N, Zhang J, Klose R J, et al. The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase[J]. Nat Struct Mol Biol,2007,14:341-343;doi: 101038/nsmb1216.
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