Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark (original) (raw)

• Chi, P., Allis, C.D. & Wang, G.G. Covalent histone modifications—miswritten, misinterpreted and mis-erased in human cancers. Nat. Rev. Cancer 10, 457–469 (2010).
  Article CAS Google Scholar
• Berger, S.L. The complex language of chromatin regulation during transcription. Nature 447, 407–412 (2007).
  Article CAS Google Scholar
• Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838–849 (2005).
  Article CAS Google Scholar
• Heintzman, N.D. et al. Distinct and predictive chromatin signatures of transcriptional promoters and enhancers in the human genome. Nat. Genet. 39, 311–318 (2007).
  Article CAS Google Scholar
• Montellier, E., Rousseaux, S., Zhao, Y. & Khochbin, S. Histone crotonylation specifically marks the haploid male germ cell gene expression program post-meiotic male-specific gene expression. Bioessays 34, 187–193 (2012).
  Article CAS Google Scholar
• Montellier, E. et al. Chromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2B. Genes Dev. 27, 1680–1692 (2013).
  Article CAS Google Scholar
• Tan, M. et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146, 1016–1028 (2011).
  Article CAS Google Scholar
• Park, J. et al. SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol. Cell 50, 919–930 (2013).
  Article CAS Google Scholar
• Xie, Z. et al. Lysine succinylation and lysine malonylation in histones. Mol. Cell. Proteomics 11, 100–107 (2012).
  Article CAS Google Scholar
• Chen, Y. et al. Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell. Proteomics 6, 812–819 (2007).
  Article CAS Google Scholar
• Chen, Y., Chen, W., Cobb, M.H. & Zhao, Y. PTMap—a sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites. Proc. Natl. Acad. Sci. USA 106, 761–766 (2009).
  Article CAS Google Scholar
• Rohwerder, T. & Mueller, R.H. Biosynthesis of 2-hydroxyisobutyric acid (2-HIBA) from renewable carbon. Microb. Cell Fact. 9, 13 (2010).
  Article Google Scholar
• Kumps, A., Duez, P. & Mardens, Y. Metabolic, nutritional, iatrogenic, and artifactual sources of urinary organic acids: a comprehensive table. Clin. Chem. 48, 708–717 (2002).
  CAS PubMed Google Scholar
• Freitas, M.A., Sklenar, A.R. & Parthun, M.R. Application of mass spectrometry to the identification and quantification of histone post-translational modifications. J. Cell. Biochem. 92, 691–700 (2004).
  Article CAS Google Scholar
• Wisniewski, J.R., Zougman, A. & Mann, M. Nɛ formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function. Nucleic Acids Res. 36, 570–577 (2008).
  Article CAS Google Scholar
• Olsen, J.V. et al. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signaling 3, ra3 (2010).
  Article Google Scholar
• Drogaris, P. et al. Histone deacetylase inhibitors globally enhance H3/H4 tail acetylation without affecting H3 lysine 56 acetylation. Sci. Rep. 2, 220 (2012).
  Article Google Scholar
• Gorovsky, M.A. et al. Histones and chromatin structure in Tetrahymena macro- and micronuclei. Cold Spring Harb. Symp. Quant. Biol. 42, 493–503 (1978).
  Article CAS Google Scholar
• Morinière, J. et al. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461, 664–668 (2009).
  Article Google Scholar
• Gaucher, J. et al. Bromodomain-dependent stage-specific male genome programming by Brdt. EMBO J. 31, 3809–3820 (2012).
  Article CAS Google Scholar
• Turner, J.M.A. Meiotic sex chromosome inactivation. Development 134, 1823–1831 (2007).
  Article CAS Google Scholar
• Namekawa, S.H. et al. Postmeiotic sex chromatin in the male germline of mice. Curr. Biol. 16, 660–667 (2006).
  Article CAS Google Scholar
• Reynard, L.N. & Turner, J.M.A. Increased sex chromosome expression and epigenetic abnormalities in spermatids from male mice with Y chromosome deletions. J. Cell Sci. 122, 4239–4248 (2009).
  Article CAS Google Scholar
• Maxwell, P.H. et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271–275 (1999).
  Article CAS Google Scholar
• Katada, S., Imhof, A. & Sassone-Corsi, P. Connecting threads: epigenetics and metabolism. Cell 148, 24–28 (2012).
  Article CAS Google Scholar
• Kaelin, W.G. & McKnight, S.L. Influence of metabolism on epigenetics and disease. Cell 153, 56–69 (2013).
  Article CAS Google Scholar
• Garcia, B.A. et al. Chemical derivatization of histones for facilitated analysis by mass spectrometry. Nat. Protoc. 2, 933–938 (2007).
  Article CAS Google Scholar
• Pivot-Pajot, C. et al. Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein. Mol. Cell. Biol. 23, 5354–5365 (2003).
  Article CAS Google Scholar
• Kotaja, N. et al. Preparation, isolation and characterization of stage-specific spermatogenic cells for cellular and molecular analysis. Nat. Methods 1, 249–254 (2004).
  Article CAS Google Scholar
• Zhang, Z. et al. Identification of lysine succinylation as a new post-translational modification. Nat. Chem. Biol. 7, 58–63 (2011).
  Article CAS Google Scholar