Identification of Histone Lysine Glutarylation

  • Xiucong BaoEmail author
Part of the Springer Theses book series (Springer Theses)


Cell signaling networks that are involved in regulation of almost all cellular functions are regulated by protein posttranslational modifications (PTMs) [1].


  1. 1.
    Choudhary C, Weinert BT, Nishida Y, Verdin E, Mann M (2014) The growing landscape of lysine acetylation links metabolism and cell signalling. Nat Rev Mol Cell Biol 15:536–550. Scholar
  2. 2.
    Walsh C (2006) Posttranslational modification of proteins: expanding nature’s inventory. Roberts and Company Publishers, Englewood, COGoogle Scholar
  3. 3.
    Walsh CT, Garneau-Tsodikova S, Gatto GJ Jr (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem 44:7342–7372. Scholar
  4. 4.
    Tan M et al (2011) Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146:1016–1028.
  5. 5.
    Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y (2011) Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol 7:58–63. Scholar
  6. 6.
    Colak G et al (2013) Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli. Mol Cell Proteomics MCP 12:3509–3520. Scholar
  7. 7.
    Du J et al (2011) Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334:806–809.
  8. 8.
    Peng C et al (2011) The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics MCP 10(M111):012658. Scholar
  9. 9.
    Verdin E, Ott M (2015) 50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond. Nat Rev Mol Cell Biol 16:258–264.
  10. 10.
    Tan M et al (2014) Lysine glutarylation is a protein posttranslational modification regulated by SIRT5. Cell Metab 19:605–617.
  11. 11.
    Brownell JE, Allis CD (1995) An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc Natl Acad Sci U S A 92:6364–6368Google Scholar
  12. 12.
    Yang YY, Ascano JM, Hang HC (2010) Bioorthogonal chemical reporters for monitoring protein acetylation. J Am Chem Soc 132:3640–3641. Scholar
  13. 13.
    Thinon E, Hang HC (2015) Chemical reporters for exploring protein acylation. Biochem Soc Trans 43:253–261. Scholar
  14. 14.
    Bao X, Zhao Q, Yang T, Fung YM, Li XD (2013) A chemical probe for lysine malonylation. Angew Chem 52:4883–4886. Scholar
  15. 15.
    Wilson JP, Raghavan AS, Yang YY, Charron G, Hang HC (2011) Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants. Mol Cell Proteomics MCP 10:M110 001198.
  16. 16.
    Xie Z et al (2012) Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics MCP 11:100–107. Scholar
  17. 17.
    Fidlerova H, Kalinova J, Blechova M, Velek J, Raska I (2009) A new epigenetic marker: the replication-coupled, cell cycle-dependent, dual modification of the histone H4 tail. J Struct Biol 167:76–82.
  18. 18.
    Ye J et al (2005) Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly. Mol Cell 18:123–130Google Scholar
  19. 19.
    Masumoto H, Hawke D, Kobayashi R, Verreault A (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436:294–298.
  20. 20.
    Ozdemir A, Spicuglia S, Lasonder E, Vermeulen M, Campsteijn C, Stunnenberg HG, Logie C (2005) Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae. J Biol Chem 280:25949–25952.
  21. 21.
    Zhang L, Eugeni EE, Parthun MR, Freitas MA (2003) Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112:77–86. Scholar
  22. 22.
    Manohar M et al (2009) Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding. J Biol Chem 284:23312–23321.
  23. 23.
    Recht J et al (2006) Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis. Proc Natl Acad Sci U S A 103:6988–6993.
  24. 24.
    Han J, Zhou H, Li Z, Xu RM, Zhang Z (2007) Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity. J Biol Chem 282:28587–28596.
  25. 25.
    Hiraga S, Botsios S, Donaldson AD (2008) Histone H3 lysine 56 acetylation by Rtt109 is crucial for chromosome positioning. J Cell Biol 183:641–651.
  26. 26.
    Shechter D, Dormann HL, Allis CD, Hake SB (2007) Extraction, purification and analysis of histones. Nat Protoc 2:1445–1457.

Copyright information

© Springer Nature Singapore Pte Ltd. 2020

Authors and Affiliations

  1. 1.Department of ChemistryThe University of Hong KongHong KongChina

Personalised recommendations