Histone is one of critical components of chromatin, which amino acid residues at the N-terminus can be covalently modified. Histone modification (HM) can change the chromatin conformation and induce transcription or gene silencing. Not only can HM control gene expression, but also participate in cell division, cell apoptosis and memory formation by recruiting protein complex and affecting downstream proteins. HM can also have the impact on immune system and inflammatory reaction. In addition, lots of recent studies have indicated that histone code (or HM) is related to the CTD code, circadian clock and DNA repair, implying the significance of HM. The domains of protein complex can never be replaced, because they play a mediating role during the formation and deciphering of histone code, as well as the modification cascade and the recruitment of protein complex. Therefore, these domains are very important to comprehend the histone code. Because of the widespread use of analytical techniques, such as mass-spectrometry, new domains will be discovered. Herein, our review focuses on the basic concept, recent progress and hot points of the histone code study.
[1] Li G, Reinberg D. Chromatin higher-order structures and gene regulation. Curr Opin Genet Dev, 2011, 21(2): 175-186.
[2] Stral BD, Allis CD. The language of covalent histone modifications. Nature, 2000, 403(6765): 41-45.
[3] Thomas J, Allis CD. Translating the histone code. Science, 2001, 293(5532):1074- 1080.
[4] Thorne AW, Sautiere P, Briand G, Crane-Robinson C. The structure of ubiquitinated histone H2B. EMBO J, 1987, 6(4): 1005-1010.
[5] Shimada M, Nakadai T, Fukuda A, Hisatake K. cAMP-response element-binding (CREB) controls MSK1-mediated phosphorylation of histone H3 at the c-fos pro-moter in vitro. J Biol Chem, 2010, 285(13): 9390-9401.
[6] Yun M, Wu J, Jerry LW, Li B. Readers of histone modifications. Cell Res, 2011, 21 (4): 564-578.
[7] Shen X. Chromatin and Epigenetic Regulation. Beijing: Higher Education Press, 2006: 104.
[8] Mellor J. It Takes a PHD to Read the Histone Code. Cell, 2006, 126(1): 22-24.
[9] David PF, Matthew JS. HDACs and their inhibitors in immunology: teaching anticancer drugs new tricks. Immunol Cell Biol, 2012, 90(1): 3-5.
[10] Gupta S, Kim SY, Artis S, Molfese DL, Schumacher A, Sweatt JD, Paylor RE, Lubin FD. Histone methylation regulates memory formation. J Neurosci, 2010, 30(10): 3589-3599.
[11] Nilanjana C, Divya S, Mekonnen LD, Song T, Michael AS, Blaine B. Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms. Nucleic Acids Res. 2011, 39(19): 8378-8391.
[12] Wu J, Michael SY, Lu L, Ye L, Dou Y, Mats L, Chen J, Yu X. Histone ubiquitination associates with BRCA1-dependent DNA damage response. Mol Cell Biol, 2009, 29(3): 849- 860.
[13] Priscilla N, Peter C. Histone code pathway involving H3 S28 phosphorylation and K27 acetylation activates tran-scription and antagonizes polycomb silencing. Proc Natl Acad Sci USA, 2011, 108(7): 2801-2806.
[14] Banerjee T, Chakravarti D. A peek into the complex realm of histone phosphorylation. Mol Cell Biol, 2011, 31(24): 4858-4873.
[15] Hasan S, Hottiger MO. Histone acetyl transferases: a role in DNA repair and DNA replication. J Mol Med, 2002, 80(8): 463-474.
[16] Gao L, Cueto MA, Asselbergs F, Atadja P. Cloning and functional characterization of HDAC 11, a novel member of the human histone deacetylase family. J Biol Chem, 2002, 277(28): 25748-25755.
[17] Grozinger M, Schreiber SL. Deacetylase enzyme: biological functions and the use of small- molecule inhibitors. Chem Biol, 2002, 9(1): 3-16.
[18] Shi YJ, Lan F, Matson C, Mulligan P, Whetstine JR, Cole RA, Shi Y. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell, 2004, 119(7): 941-953.
[19] Tsukada Y, Fang J, Hediye EB, Maria EW, Christoph HB, Paul T, Zhang Y. Histone demethylation by a family of JmjC domain-containing proteins. Nature, 2006, 439(7078): 811 -816.
[20] Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem, 2001, 70: 503- 533.
[21] Chung C, Sung H. Deubiquitinating enzymes: Their diversity and emerging roles. Biochem Biophys Res Com-mun, 1999, 266(3): 633-640.
[22] Wang F, Dai J, John RD, Ewa N, Budhaditya B, Todd S, Gary JG, Jonathan MG. Histone H3 Thr -3 phosphorylation by Haspin positions Aurora B at centromeres in mitosis. Science, 2010, 330(6001): 231-235.
[23] Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM. Structure and ligand of a histone acetyltrans-ferase bromodomain. Nature, 1999, 399(6735): 491-496.
[24] Bedford MT. Using protein domain microarrays to read the histone code. J Biomol Tech, 2011, 22(Supplement): S6-S7.
[25] Hoppmann V, Thorstensen T, Kristiansen PE, Veiseth SV, Rahman MA, Finne K, Aalen RB, Aasland R. The CW domain, a new histone recognition module in chromatin proteins