Long-range histone acetylation: Biological significance, structural implications, and mechanisms

Biochemistry and Cell Biology

Volumn 84, Issue 4, 2006, Pages 518-527

  Calestagne Morelli, Alison ^a   Ausió, Juan ^a  

^a UNIVERSITY OF VICTORIA   (Canada)

Author keywords

Chromatin; Histone acetylation; Long range; Transcription

Indexed keywords

DNA SEQUENCES; GENES; GENETIC ENGINEERING; PROTEINS;

CHROMATIN; HISTONE ACETYLATION; LONG-RANGE; TRANSCRIPTION;

ACETYLATION;

ALPHA GLOBIN; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE;

ACETYLATION; CHIMERA; CHROMATIN IMMUNOPRECIPITATION; CHROMATIN STRUCTURE; CONFERENCE PAPER; DNA CROSS LINKING; EUKARYOTE; GENE CLUSTER; GENE CONTROL; GENE EXPRESSION; GENETIC TRANSCRIPTION; NONHUMAN;

ACETYLATION; ANIMALS; CHICKENS; GLOBINS; HISTONES; MODELS, BIOLOGICAL; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSCRIPTION, GENETIC;

EUKARYOTA;

EID: 33750732646     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/O06-067     Document Type: Conference Paper

References (86)

1. Allfrey, V.G., Faulkner, R., and Mirsky, A.E. 1964. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 51: 786-794. PMID: 14172992.
2. Anderson, J.D., Lowary, P.T., and Widom, J. 2001. Effects of histone acetylation on the equilibrium accessibility of nucleosomal DNA targets. J. Mol. Biol. 307: 977-985. doi:10.1006/jmbi. 2001.4528. PMID: 11286549.
3. Anguita, E., Johnson, C.A., Wood, W.G., Turner, B.M., and Higgs, D.R. 2001. Identification of a conserved erythroid specific domain of histone acetylation across the α-globin gene cluster. Proc. Natl. Acad. Sci. U.S.A. 98: 12114-12119. doi:10.1073/pnas.201413098. PMID: 11593024.
4. Annunziato, A.T., and Hansen, J.C. 2000. Role of histone acetylation in the assembly and modulation of chromatin structures. Gene Expr. 9: 37-61. PMID: 11097424.
5. Ausió, J., and Abbott, D.W. 2004. The Role of histone variability in chromatin stability and folding. In Chromatin structure and dynamics: state-of-the-art. Edited by J. Zlanatova and S.H. Leuba. Elsevier, Amsterdam. pp. 241-290.
6. Ausió, J., and van Holde, K.E. 1986. Histone hyperacetylation: its effects on nucleosome conformation and stability. Biochemistry, 25: 1421-1428. doi:10.1021/bi00354a035. PMID: 3964683.
7. Baer, B.W., and Rhodes, D. 1983. Eukaryotic RNA polymerase II binds to nucleosome cores from transcribed genes. Nature (London), 301: 482-488. doi:10.1038/301482a0. PMID: 6823327.
8. Baxter, E.W., Cummings, W.J., and Fournier, R.E. 2005. Formation of a large, complex domain of histone hyperacetylation at human 14q32.1 requires the serpin locus control region. Nucleic Acids Res. 33: 3313-3322. doi:10.1093/nar/gki645. PMID: 15942032.
9. Belotserkovskaya, R., Oh, S., Bondarenko, V.A., Orphanides, G., Studitsky, V.M., and Reinberg, D. 2003. FACT facilitates transcription-dependent nucleosome alteration. Science (Washington, D.C.), 301: 1090-1093. doi:10.1126/science.1085703. PMID: 12934006.
10. Bernstein, B.E., Kamal, M., Lindblad-Toh, K., Bekiranov, S., Bailey, D.K., Huebert, D.J., et al. 2005. Genomic maps and comparative analysis of histone modifications in human and mouse. Cell, 120: 169-181. doi:10.1016/j.cell.2005.01.001. PMID: 15680324.
11. Brower-Toland, B., Wacker, D.A., Fulbright, R.M., Lis, J.T., Kraus, W.L., and Wang, M.D. 2005. Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes. J. Mol. Biol. 346: 135-146. PMID: 15663933.
12. Bruce, K., Myers, F.A., Mantouvalou, E., Lefevre, P., Greaves, I., Bonifer, C., et al. 2005. The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. Nucleic Acids Res. 33: 5633-5639. doi:10.1093/nar/gki874. PMID: 16204459.
13. Bruno, M., Flaus, A., Stockdale, C., Rencurel, C., Ferreira, H., and Owen-Hughes, T. 2003. Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities. Mol. Cell, 12: 1599-1606. doi:10.1016/S1097-2765(03) 00499-4. PMID: 14690611.
14. Bulger, M., Schubeler, D., Bender, M.A., Hamilton, J., Farrell, C.M., Hardison, R.C., and Groudine, M. 2003. A complex chromatin landscape revealed by patterns of nuclease sensitivity and histone modification within the mouse beta-globin locus. Mol. Cell. Biol. 23: 5234-5244. doi:10.1128/MCB.23.15.5234- 5244. 2003. PMID: 12861010.
15. Buttinelli, M., Minnock, A., Panetta, G., Waring, M., and Travers, A. 1998. The exocyclic groups of DNA modulate the affinity and positioning of the histone octamer. Proc. Natl. Acad. Sci. U.S.A. 95: 8544-8549. doi:10.1073/pnas.95.15.8544. PMID: 9671714.
16. Chambeyron, S., and Bickmore, W.A. 2004. Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription. Genes Dev. 18: 1119-1130. doi:10.1101/gad.292104. PMID: 15155579.
17. Chang, S., and Aune, T.M. 2005. Histone hyperacetylated domains across the Ifng gene region in natural killer cells and T cells. Proc. Natl. Acad. Sci. U.S.A. 102: 17095-17100. doi:10.1073/pnas.0502129102. PMID: 16286661.
18. Chowdhury, D., and Sen, R. 2001. Stepwise activation of the immunoglobin μ heavy chain gene locus. EMBO J. 20: 6394-6403. doi:10.1093/emboj/20.22. 6394. PMID: 11707410.
19. Dion, M.F., Altschuler, S.J., Wu, L.F., and Rando, O.J. 2005. Genomic characterization reveals a simple histone H4 acetylation code. Proc. Natl. Acad. Sci. U.S.A. 102: 5501-5506. doi:10.1073/pnas.0500136102. PMID: 15795371.
20. Dong, F., and van Holde, K.E. 1991. Nucleosome positioning is determined by the (H3-H4)2 tetramer. Proc. Natl. Acad. Sci. U.S.A. 88: 10596-10600. PMID: 1961726.
21. Dunker, A.K., Lawson, J.D., Brown, C.J., Williams, R.M., Romero, P., Oh, J.S., et al. 2001. Intrinsically disordered protein. J. Mol. Graph. Model. 19: 26-59. PMID: 11381529.
22. Eberharter, A., and Becker, P.B. 2002. Histone acetylation: a switch between repressive and permissive chromatin. Second in review series on chromatin dynamics. EMBO Rep. 3: 224-229. doi:10.1093/embo-reports/kvf053. PMID: 11882541.
23. Elefant, F., Cooke, N.B., and Liebhaber, S.A. 2000a. Targeted recruitment of histone acetyltransferase activity to a locus control region. J. Biol. Chem. 275: 13 827-13 834. doi:10.1074/jbc.275.18.13827. PMID: 10788505.
24. Elefant, F., Su, Y., Liebhaber, S.A., and Cooke, N.E. 2000b. Patterns of histone acetylation suggest dual pathways for gene activation by a bifunctional locus control region. EMBO J. 19: 6814-6822. doi:10.1093/emboj/19.24.6814. PMID: 11118216.
25. Forsberg, E.C., Downs, K.M., Christensen, H.M., Im, H., Nuzzi, P.A., and Bresnick, E.H. 2000. Developmentally dynamic histone acetylation pattern of a tissue-specific chromatin domain. Proc. Natl. Acad. Sci. U.S.A. 97: 14 494-14 499. doi:10.1073/pnas.97.26.14494. PMID: 11121052.
26. Garcia-Ramirez, M., Rocchini, C., and Ausió, J. 1995. Modulation of chromatin folding by histone acetylation. J. Biol. Chem. 270: 17 923-17 928. PMID: 7629098.
27. Gorisch, S.M., Wachsmuth, M., Toth, K.P., Lichter, P., and Rippe, K. 2005. Histone acetylation increases chromatin accessibility. J. Cell Sci. 118: 5825-5834. doi:10.1242/jcs.02689. PMID: 16317046.
28. Hebbes, T.R., Clayton, A.L., Thorne, A.W., and Crane-Robinson, C. 1994. Core histone hyperacetylation co-maps with generalized DNase I sensitivity in the chicken beta-globin chromosomal domain. EMBO J. 13: 1823-1830. PMID: 8168481.
29. Howe, L., and Ausió, J. 1998. Nucleosome translation position, not histone acetylation determines TFIIA binding to nucleosomal Xenopus laevis 5S rRNA genes. Mol. Cell. Biol. 18: 1156-1162. PMID: 9488430.
30. Jackson, V. 1990. In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both. Biochemistry, 29: 719-731. doi:10.1021/bi00455a019. PMID: 1692479.
31. Jenuwein, T., and Allis, C.D. 2001. Translating the histone code. Science (Washington, D.C.), 293: 1074-1080. doi:10.1126/science.1063127. PMID: 11498575.
32. Kamakaka, R.T., and Thomas, J.O. 1990. Chromatin structure of transcriptionally competent and repressed genes. EMBO J. 9: 3997-4006. PMID: 2249661.
33. Katan-Khaykovich, Y., and Struhl, K. 2002. Dynamics of global histone acetylation and deacetylation in vivo: rapid restoration of normal histone acetylation status upon removal of activators and repressors. Genes Dev. 16: 743-752. doi:10.1101/gad. 967302. PMID: 11914279.
34. Kimura, A.P., Liebhaber, S.A., and Cooke, N.B. 2004. Epigenetic modifications at the human growth hormone locus predict distinct roles for histone acetylation and methylation in placental gene activation. Mol. Endocrinol. 18: 1018-1032. doi:10.1210/me.2003-0468. PMID: 14715931.
35. Kimura, T., Mills, P.C., Allan, J., and Gould, H. 1983. Selective unfolding of erythroid chromatin in the region of the active beta-globin gene. Nature (London), 306: 709-712. doi:10.1038/306709a0. PMID: 6656872.
36. Kireeva, M.L., Walter, W., Tchernajenko, V., Bondarenko, V., Kashlev, M., and Studitsky, V.M. 2002. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol. Cell, 9: 541-552. doi:10.1016/S1097-2765(02)00472-0. PMID: 11931762.
37. Korzus, E., Torchia, J., Rose, D.W., Xu, L., Kurokawa, R., McInerney, E.M., et al. 1998. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science (Washington, D.C.), 279: 703-707. doi:10.1126/science.279. 5351.703. PMID: 9445475.
38. Krajewski, W.A., and Becker, P.B. 1998. Reconstitution of hyperacetylated, DNase I-sensitive chromatin characterized by high conformational flexibility of nucleosomal DNA. Proc. Natl. Acad. Sci. U.S.A. 95: 1540-1545. doi:10.1073/pnas.95.4.1540. PMID: 9465051.
39. Krebs, J.E., Fry, C.J., Samuels, M.L., and Peterson, C.L. 2000. Global role for chromatin remodeling enzymes in mitotic gene expression. Cell, 102: 587-598. doi:10.1016/S0092-8674(00) 00081-7. PMID: 11007477.
40. Kuo, M.H., vom Baur, E., Struhl, K., and Allis, C.D. 2000. Gcn4 activator targets Gcn5 histone acetyltransferase to specific promoters independently of transcription. Mol. Cell, 6: 1309-1320. doi:10.1016/S1097-2765(00)00129-5. PMID: 11163205.
41. Kurdistani, S.K., Tavazoie, S., and Grunstein, M. 2004. Mapping global histone acetylation patterns to gene expression. Cell, 117: 721-733. doi:10.1016/j.cell.2004.05.023. PMID: 15186774.
42. Lee, D.Y., Hayes, J.J., Pruss, D., and Wolffe, A.P. 1993. A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell, 72: 73-84. doi:10.1016/0092-8674(93) 90051-Q. PMID: 8422685.
43. Letting, D.L., Rakowski, C., Weiss, M.J., and Gerd, A.B. 2003. Formation of a tissue-specific histone acetylation pattern by the hematopoietic transcription factor GATA-1. Mol. Cell. Biol. 23: 1334-1340. doi:10.1128/MCB.23.4.1334-1340.2003. PMID: 12556492.
44. Levchenko, V., Jackson, B., and Jackson, V. 2005. Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress. Biochemistry, 44: 5357-5372. doi:10.1021/bi047786o. PMID: 15807529.
45. Li, G., Levitus, M., Bustamante, C., and Widom, J. 2005. Rapid spontaneous accessibility of nucleosomal DNA. Nat. Struct. Mol. Biol. 12: 46-53. doi:10.1038/nsmb869. PMID: 15580276.
46. Liang, G., Lin, J.C., Wei, V., Yoo, C., Cheng, J.C., Nguyen, C.T., et al. 2004. Distinct localization of histone H3 acetylation and H3-K4 methylation to the transcription start sites in the human genome. Proc. Natl. Acad. Sci. U.S.A. 101: 7357-7362. doi:10.1073/pnas.0401866101. PMID: 15123803.
47. Litt, M.D., Simpson, M., Recillas-Targa, F., Prioleau, M.N., and Felsenfeld, G. 2001. Transition in histone acetylation reveal boundaries of three separately regulated neighboring loci. EMBO J. 20: 2224-2235. doi:10.1093/emboj/20.9.2224. PMID: 11331588.
48. McGhee, J.D., Nickol, J.M., Felsenfeld, G., and Rau, D.C. 1983. Histone hyperacetylation has little effect on the higher order folding of chromatin. Nucleic Acids Res. 11: 4065-4075. PMID: 6866766.
49. Morales, V., and Richard-Foy, H. 2000. Role of N-terminal tails and their acetylation in nucleosome dynamics. Mol. Cell. Biol. 20: 7230-7237. doi:10.1128/MCB.20.19.7230-7237.2000. PMID: 10982840.
50. Mutskov, V., Gerber, D., Angelov, D., Ausió, J., Workman, J., and Dimitrov, S. 1998. Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding. Mol. Cell. Biol. 18: 6293-6304. PMID: 9774646.
51. Myers, F.A., Evans, D.R., Clayton, A.L., Thorne, A.W., and Crane-Robinson, C. 2001. Targeted and extended acetylation of histones H4 and H3 at active and inactive genes in chicken embryo erythrocytes. J. Biol. Chem. 276: 20 197-20 205. doi:10.1074/jbc.M009472200. PMID: 11274167.
52. Myers, F.A., Chong, W., Evans, D.R., Thorne, A.W., and Crane-Robinson, C. 2003. Acetylation of histone H2B mirrors that of H4 and H3 at the chicken beta-globin locus but not at housekeeping genes. J. Biol. Chem. 278: 36 315-36 322. doi:10. 1074/jbc.M305822200. PMID: 12865423.
53. Norton, V.G., Imai, B.S., Yau, P., and Bradbury, E.M. 1989. Histone acetylation reduces nucleosome core particle linking number change. Cell, 57: 449-457. doi:10.1016/0092-8674(89) 90920-3. PMID: 2541913.
54. Oliva, R., Bazett-Jones, D.P., Locklear, L., and Dixon, G.H. 1990. Histone hyperacetylation can induce unfolding of the nucleosome core particle. Nucleic Acids Res. 18: 2739-2747. PMID: 2339060.
55. Parekh, B.S., and Maniatis, T. 1999. Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter. Mol. Cell, 3: 125-129. doi:10.1016/S1097-2765(00) 80181-1. PMID: 10024886.
56. Park, Y.J., and Luger, K. 2006. The structure of nucleosome assembly protein 1. Proc. Natl. Acad. Sci. U.S.A. 103: 1248-1253. doi:10.1073/pnas. 0508002103. PMID: 16432217.
57. Perry, C.A., and Annunziato, A.T. 1991. Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly. Exp. Cell Res. 196: 337-345. doi:10.1016/0014-4827(91)90269-Z. PMID: 1893943.
58. Perry, M., and Chalkley, R. 1982. Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation. J. Biol. Chem. 257: 7336-7347. PMID: 7085629.
59. Protacio, R.U., Li, G., Lowary, P.T., and Widom, J. 2000. Effects of histone tail domains on the rate of transcriptional elongation through a nucleosome. Mol. Cell. Biol. 20: 8866-8878. doi:10.1128/MCB.20.23.8866-8878. 2000. PMID: 11073987.
60. Rastegar, M., Kobrossy, L., Kovacs, E.N., Rambaldi, I., and Featherstone, M. 2004. Sequential histone modifications at Hoxd4 regulatory regions distinguish anterior from posterior embryonic compartments. Mol. Cell. Biol. 24: 8090-8103. doi:10.1128/MCB.24.18.8090-8103.2004. PMID: 15340071.
61. Reid, J.L., Moqtaderi, Z., and Struhl, K. 2004. Eaf3 regulates the global pattern of histone acetylation in Saccharomyces cerevisiae. Mol. Cell. Biol. 24: 757-764. doi:10.1128/MCB.24.2.757-764.2004. PMID: 14701747.
62. Ridsdale, J.A., Hendzel, M.J., Delcuve, G.P., and Davie, J.R. 1990. Histone acetylation alters the capacity of the H1 histones to condense transcriptionally active/competent chromatin. J. Biol. Chem. 265: 5150-5156. PMID: 2318888.
63. Roh, T.Y., Cuddapah, S., and Zhao, K. 2005. Active chromatin domains are defined by acetylation islands revealed by genome-wide mapping. Genes Dev. 19: 542-552. doi:10.1101/gad.1272505. PMID: 15706033.
64. Roh, T.Y., Ngau, W.C., Cui, K., Landsman, D., and Zhao, K. 2004. High-resolution genome-wide mapping of histone modifications. Nat. Biotechnol. 22: 1013-1016. doi:10.1038/nbt990. PMID: 15235610.
65. Schubeler, D., Francastel, C., Cimbora, D.M., Reik, A., Martin, D.I., and Groudine, M. 2000. Nuclear localization and histone acetylation: a pathway for chromatin opening and transcriptional activation of the human beta-globin locus. Genes Dev. 14: 940-950. PMID: 10783166.
66. Schubeler, D., MacAlpine, D.M., Scalzo, D., Wirbelauer, C., Kooperberg, C., van Leeuwen, F., et al. 2004. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev. 18: 1263-1271. doi:10.1101/gad.1198204. PMID: 15175259.
67. Sewack, G.F., Ellis, T.W., and Hansen, U. 2001. Binding of TATA binding protein to a naturally positioned nucleosome is facilitated by histone acetylation. Mol. Cell. Biol. 21: 1404-1415. doi:10.1128/MCB.21.4.1404-1415. 2001. PMID: 11158325.
68. Shogren-Knaak, M., Ishii, H., Sun, J.M., Pazin, M.J., Davie, J.R., and Peterson, C.L. 2006. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science (Washington, D.C.), 311: 844-847. doi:10.1126/science.H24000. PMID: 16469925.
69. Siino, J.S., Yau, P.M., Imai, B.S., Gatewood, J.M., and Bradbury, E.M. 2003. Effect of DNA length and H4 acetylation on the thermal stabilty of reconstituted nucleosome particles. Biochem. Biophys. Res. Commun. 302: 885-891. doi:10.1016/S0006-291X(03)00277-8. PMID: 12646255.
70. Simpson, R.T. 1978. Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry, 17: 5524-5531. doi:10.1021/bi00618a030. PMID: 728412.
71. Strahl, B.D., and Allis, C.D. 2000. The language of covalent histone modifications. Nature (London), 403: 41-45. PMID: 10638745.
72. Thorne, A.W., Kmiciek, D., Mitchelson, K., Sautiere, P., and Crane-Robinson, C. 1990. Patterns of histone acetylation. Eur. J. Biochem. 193: 701-713. doi:10.1111/j.1432-1033.1990. tb19390.x. PMID: 2249688.
73. Tomschik, M., Zheng, H., van Holde, K., Zlatanova, J., and Leuba, S.H. 2005. Fast, long-range, reversible conformational fluctuations in nucleosomes revealed by single-pair fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 102: 3278-3283. doi:10.1073/pnas.0500189102. PMID: 15728351.
74. Topalidou, I., Papamichos-Chronakis, M., and Thireos, G. 2003. Post-TATA binding protein recruitment clearance of Gcn5-dependent histone acetylation within promoter nucleosomes. Mol. Cell. Biol. 23: 7809-7817. doi:10.1128/MCB.23.21.7809-7817. 2003. PMID: 14560024.
75. Tse, C., Sera, T., Wolffe, A.P., and Hansen, J.C. 1998. Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol. Cell. Biol. 18: 4629-4638. PMID: 9671473.
76. Turner, B.M. 2005. Reading signals on the nucleosome with a new nomenclature for modified histones. Nat. Struct. Mol. Biol. 12: 110-112. doi:10.1038/nsmb0205-110. PMID: 15702071.
77. van Holde, K.E. 1989. Chromatin. Springner Verlag, NewYork.
78. van Holde, K.E., Lohr, D.E., and Robert, C. 1992. What happens to nucleosomes during transcription? J. Biol. Chem. 267: 2837-2840. PMID: 1310672.
79. Vignali, M., Steger, D.J., Neely, K.E., and Workman, J.L. 2000. Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes. EMBO J. 19: 2629-2640. PMID: 10835360.
80. Vogelauer, M., Wu, J., Suka, N., and Grunstein, M. 2000. Global histone acetylation and deacetylation in yeast. Nature (London), 408: 495-498. PMID: 11100734.
81. Wang, X., Moore, S.C., Laszckzak, M., and Ausio, J. 2000. Acetylation increases the α-helical content of the histone tails of the nucleosome. J. Biol. Chem. 275: 35 013-35 020. doi:10.1074/jbc.M004998200. PMID: 10938086.
82. Wang, X., He, C., Moore, S.C., and Ausió, J. 2001. Effects of histone acetylation on the solubility and folding of the chromatin fiber. J. Biol. Chem. 276: 12 764-12 768. doi:10.1074/jbc.M100501200. PMID: 11279082.
83. Waterborg, J.H. 2000. Steady-state levels of histone acetylation in Saccharomyces cerevisiae. J. Biol. Chem. 275: 13 007-13 011. doi:10.1074/jbc.275.17.13007. PMID: 10777603.
84. Waterborg, J.H. 2002. Dynamics of histone acetylation in vivo. A function for acetylation turnover? Biochem. Cell Biol. 80: 363-378. doi:10.1139/002-080. PMID: 12123289.
85. Zhang, K., Williams, K.E., Huang, L., Yau, P., Siino, J.S., Bradbury, E.M., et al. 2002. Histone acetylation and deacetylation: identification of acetylation and methylation sites of HeLa histone H4 by mass spectrometry. Mol. Cell. Proteomoics: MCP, 1: 500-508.
86. Zhou, W., Chang, S., and Aune, T.M. 2004. Long-range histone acetylation of the Ifng gene is an essential feature of T cell differentiation. Proc. Natl. Acad. Sci. U.S.A. 101: 2440-2445. doi:10.1073/pnas.0306002101. PMID: 14983028.