ubiquitinylation succinylation butyrylation hydroxylation crotonylation
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1 Supplementary Information S1 (table) Overview of histone core-modifications histone, residue/modification H1 H2A methylation acetylation phosphorylation formylation oxidation crotonylation hydroxylation ubiquitinylation succinylation butyrylation citrullination propionylation proposed function K46 1 K48 oxidative damage (formyl) 1,2 R54 chromatin compaction, transcription 3 K65 oxidative damage (formyl) 2,4 K66 oxidative damage (formyl) 2,4 Y73 4 K83 oxidative damage (formyl) 4 K87 oxidative damage (formyl) 4 K92 oxidative damage (formyl) 1,4 K99 1 K36 4,5 Y39 4 R42 4 K74 6 K75 6 R77 6 R88 4 K95 6 Q105 rdna transcription 7 Ref. 1
2 H2B H3 K20 transcription 4 K23 4 K30 S33 K34 oxidative damage (formyl) 2,4,8 Y37 4 K43 5 K46 oxidative damage (formyl) 2,5 K57 4 R79 4 Y83 4 K85 4 R99 4 Y41 transcription 9 R42 transcription 10 T45 apoptosis 11 transcription, replication, DNA and oxidative damage (formyl) 4, K56 S57 16 R63 4 K64 transcription 4,6,17 transcription, oxidative damage K79 (formyl) 2,18-20 T80 mitosis 16 K122 R128 transcription, oxidative damage (formyl) 2,4,21 4 2
3 H4 K20 4 K31 oxidative damage (formyl) 2,4,22 R35 4 K44 22 S47 nucleosome assembly 23 Y51 4 R55 4 K59 oxidative damage (formyl) 2,4 R67 4 K77 4 K79 oxidative damage (formyl) 2,4 Y88 4 K91 replication, DNA damage 4 R92 4,6 References 1. Wisniewski, J. R., Zougman, A., Krüger, S. & Mann, M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol. Cell Proteomics 6, (2007). 2. Jiang, T., Zhou, X., Taghizadeh, K., Dong, M. & Dedon, P. C. N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage. Proc Natl Acad Sci USA 104, (2007). 3. Christophorou, M. A. et al. Citrullination regulates pluripotency and histone H1 binding to chromatin. Nature 507, (2014). 4. Tan, M. et al. Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification. Cell 146, (2011). 5. Zhang, L., Eugeni, E. E., Parthun, M. R. & Freitas, M. A. Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112, (2003). 6. Freitas, M. A., Sklenar, A. R. & Parthun, M. R. Application of mass spectrometry to the identification and quantification of histone posttranslational modifications. J Cell Biochem 92, (2004). 3
4 7. Tessarz, P. et al. Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification. Nature 505, (2014). 8. Xie, Z. et al. Lysine Succinylation and Lysine Malonylation in Histones. Mol. Cell Proteomics 11, (2012). 9. Dawson, M. A. et al. JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature 461, (2009). 10. Casadio, F., Lu, X., Pollock, S. B. & LeRoy, G. H3R42me2a is a histone modification with positive transcriptional effects. Proc. Natl Acad. Sci. USA 110, (2013) 11. Hurd, P. J. et al. Phosphorylation of Histone H3 Thr-45 Is Linked to Apoptosis. Journal of Biological Chemistry 284, (2009). 12. Xu, F., Zhang, K. & Grunstein, M. Acetylation in Histone H3 Globular Domain Regulates Gene Expression in Yeast. Cell 121, (2005). 13. Ozdemir, A. Characterization of Lysine 56 of Histone H3 as an Acetylation Site in Saccharomyces cerevisiae. Journal of Biological Chemistry 280, (2005). 14. Masumoto, H., Hawke, D., Kobayashi, R. & Verreault, A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436, (2005). 15. Yu, Y. et al. Histone H3 Lysine 56 Methylation Regulates DNA Replication through Its Interaction with PCNA. Mol. Cell 46, 7-17 (2012) 16. Vermeulen, M. et al. Quantitative Interaction Proteomics and Genome-wide Profiling of Epigenetic Histone Marks and Their Readers. Cell 142, (2010). 17. Di Cerbo, V. et al. Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription. elife 3, e01632 e01632 (2014). 18. Schübeler, D. et al. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes & Development 18, (2004). 19. Vakoc, C. R., Sachdeva, M. M., Wang, H. & Blobel, G. A. Profile of Histone Lysine Methylation across Transcribed Mammalian Chromatin. Molecular and Cellular Biology 26, (2006). 20. Steger, D. J. et al. DOT1L/KMT4 Recruitment and H3K79 Methylation Are Ubiquitously Coupled with Gene Transcription in Mammalian Cells. Molecular and Cellular Biology 28, (2008). 21. Tropberger, P. et al. Regulation of Transcription through Acetylation of H3K122 on the Lateral Surface of the Histone Octamer. Cell 152, (2013). 22. Chen, Y. et al. Lysine Propionylation and Butyrylation Are Novel Post-translational Modifications in Histones. Molecular & Cellular Proteomics 6, (2007). 4
5 23. Kang, B. et al. Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly. Genes & Development 25, (2011). 5
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