5. Deng H, Bao X, Cai W, Blacketer MJ, Belmont AS, et al. (2008) Ectopic histone H3S10 phosphorylation causes chromatin structure remodeling in Drosophila. Development 135: 699–705. 6. Zhang W, Deng H, Bao X, Lerach S, Girton J, et al. (2006) The JIL-1 histone H3S10 kinase regulates dimethyl H3K9 modifications and heterochromatic spreading in Drosophila. Development 133: 229–235. 7. Lerach S, Zhang W, Bao X, Deng H, Girton J, et al. (2006) Loss-of-function alleles of the JIL-1 kinase are strong suppressors of position effect variegation of the wm4 allele in Drosophila. Genetics 173: 2403–2406. 8. Bao X, Deng H, Johansen J, Girton J, Johansen KM (2007) Loss-of-function alleles of the JIL-1 histone H3S10 kinase enhance position-effect variegation at pericentric sites in Drosophila heterochromatin. Genetics 176: 1355–1358. 9. Ebert A, Schotta G, Lein S, Kubicek S, Krauss V, et al. (2004) Su(var) genes regulate the balance between euchromatin and heterochromatin in Drosophila. Genes Dev 18: 2973–2983. 10. Deng H, Bao X, Zhang W, Girton J, Johansen J, et al. (2007) Reduced levels of Su(var)3-9 but not Su(var)2-5 (HP1) counteract the effects on chromatin structure and viability in loss-of-function mutants of the JIL-1 histone H3S10 kinase. Genetics 177: 79–87. 11. Deng H, Cai W, Wang C, Lerach S, Delattre M, et al. (2010) JIL-1 AND SU(VAR)3-7 Interact Genetically and Counteract Each Other’s Effect on Position Effect Variegation in Drosophila. Genetics. 12. Vermeulen L, Berghe WV, Beck IM, De Bosscher K, Haegeman G (2009) The versatile role of MSKs in transcriptional regulation. Trends Biochem Sci 34: 311–318. 13. Winter S, Simboeck E, Fischle W, Zupkovitz G, Dohnal I, et al. (2008) 14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activation. EMBO J 27: 88–99. 14. Vicent GP, Ballare C, Nacht AS, Clausell J, Subtil-Rodriguez A, et al. (2006) Induction of progesterone target genes requires activation of Erk and Msk kinases and phosphorylation of histone H3. Mol Cell 24: 367–381. 15. Macdonald N, Welburn JP, Noble ME, Nguyen A, Yaffe MB, et al. (2005) Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3. Mol Cell 20: 199–211. 16. Zippo A, Serafini R, Rocchigiani M, Pennacchini S, Krepelova A, et al. (2009) Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation. Cell 138: 1122–1136. 17. Karam CS, Kellner WA, Takenaka N, Clemmons AW, Corces VG (2010) 14-3- 3 Mediates Histone Cross-Talk during Transcription Elongation in Drosophila. PLoS Genet 6: e1000975. doi:10.1371/journal.pgen.1000975. 18. Ivaldi MS, Karam CS, Corces VG (2007) Phosphorylation of histone H3 at Ser10 facilitates RNA polymerase II release from promoter-proximal pausing in Drosophila. Genes Dev 21: 2818–2831. 19. Cai W, Bao X, Deng H, Jin Y, Girton J, et al. (2008) RNA polymerase II- mediated transcription at active loci does not require histone H3S10 phosphorylation in Drosophila. Development 135: 2917–2925. 20. Straub T, Becker PB (2007) Dosage compensation: the beginning and end of generalization. Nat Rev Genet 8: 47–57. 21. Gelbart ME, Kuroda MI (2009) Drosophila dosage compensation: a complex voyage to the X chromosome. Development 136: 1399–1410. 22. Jin Y, Wang Y, Johansen J, Johansen KM (2000) JIL-1, a chromosomal kinase implicated in regulation of chromatin structure, associates with the male specific lethal (MSL) dosage compensation complex. J Cell Biol 149: 1005–1010. 23. Alekseyenko AA, Larschan E, Lai WR, Park PJ, Kuroda MI (2006) High- resolution ChIP-chip analysis reveals that the Drosophila MSL complex selectively identifies active genes on the male X chromosome. Genes Dev 20: 848–857. 24. Gilfillan GD, Straub T, de Wit E, Greil F, Lamm R, et al. (2006) Chromosome- wide gene-specific targeting of the Drosophila dosage compensation complex. Genes Dev 20: 858–870. 25. Gelbart ME, Larschan E, Peng S, Park PJ, Kuroda MI (2009) Drosophila MSL complex globally acetylates H4K16 on the male X chromosome for dosage compensation. Nat Struct Mol Biol 16: 825–832. 26. Prestel M, Feller C, Straub T, Mitl o¨hner H, Becker PB (2010) The activation potential of MOF is constrained for doasege compensation. Molecular Cell 38: 815–826. 27. Shogren-Knaak M, Ishii H, Sun JM, Pazin MJ, Davie JR, et al. (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311: 844–847. 28. Zhang Y, Oliver B (2010) An evolutionary consequence of dosage compensation on Drosophila melanogaster female X-chromatin structure? BMC Genomics 11: 6. 29. Straub T, Grimaud C, Gilfillan GD, Mitterweger A, Becker PB (2008) The chromosomal high-affinity binding sites for the Drosophila dosage compensation complex. PLoS Genet 4: e1000302. doi:10.1371/journal.pgen.1000302. 30. Larschan E, Alekseyenko AA, Gortchakov AA, Peng S, Li B, et al. (2007) MSL complex is attracted to genes marked by H3K36 trimethylation using a sequence-independent mechanism. Mol Cell 28: 121–133. 31. Lee JS, Shilatifard A (2007) A site to remember: H3K36 methylation a mark for histone deacetylation. Mutat Res 618: 130–134. 32. Villar-Garea A, Imhof A (2008) Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster. PLoS ONE 3: e1553. doi:10.1371/journal.pone.0001553. JIL-1 and Transcriptionn 33. Boeke J, Regnard C, Cai W, Johansen J, Johansen KM, et al. (2010) Phosphorylation of SU(VAR)3-9 by the chromosomal kinase JIL-1. PLoS ONE 5: e10042. doi:10.1371/journal.pone.0010042. 34. Giet R, Glover DM (2001) Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis. J Cell Biol 152: 669–682. 35. Nowak SJ, Corces VG (2004) Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet 20: 214–220. 36. Gadea BB, Ruderman JV (2005) Aurora kinase inhibitor ZM447439 blocks chromosome-induced spindle assembly, the completion of chromosome condensation, and the establishment of the spindle integrity checkpoint in Xenopus egg extracts. Mol Biol Cell 16: 1305–1318. 37. Morales-Mulia S, Scholey JM (2005) Spindle pole organization in Drosophila S2 cells by dynein, abnormal spindle protein (Asp), and KLP10A. Mol Biol Cell 16: 3176–3186. 38. Clayton AL, Hazzalin CA, Mahadevan LC (2006) Enhanced histone acetylation and transcription: a dynamic perspective. Mol Cell 23: 289–296. 39. Clayton AL, Rose S, Barratt MJ, Mahadevan LC (2000) Phosphoacetylation of histone H3 on c-fos- and c-jun-associated nucleosomes upon gene activation. EMBO J 19: 3714–3726. 40. Brunmeir R, Lagger S, Simboeck E, Sawicka A, Egger G, et al. (2010) Epigenetic regulation of a murine retrotransposon by a dual histone modification mark. PLoS Genet 6: e1000927. doi:10.1371/journal.pgen.1000927. 41. Petesch SJ, Lis JT (2008) Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 134: 74–84. 42. Zink D, Paro R (1995) Drosophila Polycomb-group regulated chromatin inhibits the accessibility of a trans-activator to its target DNA. EMBO J 14: 5660–5671. 43. Kelley RL, Wang J, Bell L, Kuroda MI (1997) Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism. Nature 387: 195–199. 44. Dahlsveen IK, Gilfillan GD, Shelest VI, Lamm R, Becker PB (2006) Targeting determinants of dosage compensation in Drosophila. PLoS Genet 2: e5. doi:10.1371/journal.pgen.0020005. 45. Filion GJ, van Bemmel JG, Braunschweig U, Talhout W, Kind J, et al. (2010) Systematic protein location mapping reveals five principal chromatin types in Drosophila cells. Cell 143: 212–224. 46. Kind J, Vaquerizas JM, Gebhardt P, Gentzel M, Luscombe NM, et al. (2008) Genome-wide analysis reveals MOF as a key regulator of dosage compensation and gene expression in Drosophila. Cell 133: 813–828. 47. Raja SJ, Charapitsa I, Conrad T, Vaquerizas JM, Gebhardt P, et al. (2010) The nonspecific lethal complex is a transcriptional regulator in Drosophila. Molecular Cell 38: 827–841. 48. Ciurciu A, Komonyi O, Boros IM (2008) Loss of ATAC-specific acetylation of histone H4 at Lys12 reduces binding of JIL-1 to chromatin and phosphorylation of histone H3 at Ser10. J Cell Sci 121: 3366–3372. 49. Suganuma T, Gutierrez JL, Li B, Florens L, Swanson SK, et al. (2008) ATAC is a double histone acetyltransferase complex that stimulates nucleosome sliding. Nat Struct Mol Biol 15: 364–372. 50. Lo WS, Trievel RC, Rojas JR, Duggan L, Hsu JY, et al. (2000) Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5- mediated acetylation at lysine 14. Mol Cell 5: 917–926. 51. Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, et al. (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5: 905–915. 52. Rea S, Eisenhaber F, O’Carroll D, Strahl BD, Sun ZW, et al. (2000) Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406: 593–599. 53. Zippo A, De Robertis A, Serafini R, Oliviero S (2007) PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation. Nat Cell Biol 9: 932–944. 54. Winter S, Fischle W, Seiser C (2008) Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns. Cell Cycle 7: 1336–1342. 55. Fuda NJ, Ardehali MB, Lis JT (2009) Defining mechanisms that regulate RNA polymerase II transcription in vivo. Nature 461: 186–192. 56. Hager GL, McNally JG, Misteli T (2009) Transcription dynamics. Mol Cell 35: 741–753. 57. Wijgerde M, Grosveld F, Fraser P (1995) Transcription complex stability and chromatin dynamics in vivo. Nature 377: 209–213. 58. Fischle W, Tseng BS, Dormann HL, Ueberheide BM, Garcia BA, et al. (2005) Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 438: 1116–1122. 59. Hirota T, Lipp JJ, Toh BH, Peters JM (2005) Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438: 1176–1180. 60. Bao X, Zhang W, Krencik R, Deng H, Wang Y, et al. (2005) The JIL-1 kinase interacts with lamin Dm0 and regulates nuclear lamina morphology of Drosophila nurse cells. J Cell Sci 118: 5079–5087. 61. Negre N, Hennetin J, Sun LV, Lavrov S, Bellis M, et al. (2006) Chromosomal distribution of PcG proteins during Drosophila development. PLoS Biol 4: e170. doi:10.1371/journal.pbio.0040170. PLoS Genetics | www.plosgenetics.org 16 March 2011 | Volume 7 | Issue 3 | e1001327