Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark

Nature Chemical Biology

Volumn 10, Issue 5, 2014, Pages 365-370

  Dai, Lunzhi ^a   Peng, Chao ^a   Montellier, Emilie ^b   Lu, Zhike ^a   Chen, Yue ^a   Ishii, Haruhiko ^c   Debernardi, Alexandra ^b   Buchou, Thierry ^b   Rousseaux, Sophie ^b   Jin, Fulai ^c   Sabari, Benjamin R ^d   Deng, Zhiyou ^a   Allis, C David ^d   Ren, Bing ^c   Khochbin, Saadi ^b   Zhao, Yingming ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b INSERM   (France)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; LYSINE; LYSINE 2 HYDROXYISOBUTYRYLATION; UNCLASSIFIED DRUG;

ARTICLE; CELL DIFFERENTIATION; CHEMICAL STRUCTURE; CHROMATIN IMMUNOPRECIPITATION; EPIGENETICS; GENE EXPRESSION; GENE SEQUENCE; GENETIC ASSOCIATION; GENETIC TRANSCRIPTION; GENOMICS; GERM CELL; HISTONE ACETYLATION; HUMAN; IMMUNODETECTION; MALE; MEIOSIS; NONHUMAN; PRIORITY JOURNAL; SPERMATOCYTE; STOICHIOMETRY;

AMINO ACID SEQUENCE; ANIMALS; EPIGENESIS, GENETIC; GENOME; HELA CELLS; HISTONES; HUMANS; HYDROXYBUTYRATES; LYSINE; MALE; MASS SPECTROMETRY; MICE; MOLECULAR SEQUENCE DATA; SPERMATOZOA;

EID: 84899473489     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1497     Document Type: Article

References (30)

1. 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).
2. Berger, S.L. The complex language of chromatin regulation during transcription. Nature 447, 407-412 (2007). (Pubitemid 46816746)
3. Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838-849 (2005). (Pubitemid 41568733)
4. 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). (Pubitemid 46328487)
5. 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).
6. Montellier, E. et al. Chromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2B. Genes Dev. 27, 1680-1692 (2013).
7. 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).
8. Park, J. et al. SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. Mol. Cell 50, 919-930 (2013).
9. Xie, Z. et al. Lysine succinylation and lysine malonylation in histones. Mol. Cell. Proteomics 11, 100-107 (2012).
10. Chen, Y. et al. Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell. Proteomics 6, 812-819 (2007). (Pubitemid 46831933)
11. 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).
12. Rohwerder, T. & Mueller, R.H. Biosynthesis of 2-hydroxyisobutyric acid (2-HIBA) from renewable carbon. Microb. Cell Fact. 9, 13 (2010).
13. 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). (Pubitemid 34439102)
14. 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). (Pubitemid 44264260)
15. Wisniewski, J.R., Zougman, A. & Mann, M. Na 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). (Pubitemid 351250448)
16. Olsen, J.V. et al. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signaling 3, ra3 (2010).
17. Drogaris, P. et al. Histone deacetylase inhibitors globally enhance H3/H4 tail acetylation without affecting H3 lysine 56 acetylation. Sci. Rep. 2, 220 (2012).
18. Gorovsky, M.A. et al. Histones and chromatin structure in Tetrahymena macro- and micronuclei. Cold Spring Harb. Symp. Quant. Biol. 42, 493-503 (1978).
19. Morinière, J. et al. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461, 664-668 (2009).
20. Gaucher, J. et al. Bromodomain-dependent stage-specific male genome programming by Brdt. EMBO J. 31, 3809-3820 (2012).
21. Turner, J.M.A. Meiotic sex chromosome inactivation. Development 134, 1823-1831 (2007). (Pubitemid 46939228)
22. Namekawa, S.H. et al. Postmeiotic sex chromatin in the male germline of mice. Curr. Biol. 16, 660-667 (2006).
23. 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).
24. Maxwell, P.H. et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399, 271-275 (1999). (Pubitemid 29246458)
25. Katada, S., Imhof, A. & Sassone-Corsi, P. Connecting threads: epigenetics and metabolism. Cell 148, 24-28 (2012).
26. Kaelin, W.G. & McKnight, S.L. Influence of metabolism on epigenetics and disease. Cell 153, 56-69 (2013).
27. Garcia, B.A. et al. Chemical derivatization of histones for facilitated analysis by mass spectrometry. Nat. Protoc. 2, 933-938 (2007). (Pubitemid 46745589)
28. Pivot-Pajot, C. et al. Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein. Mol. Cell. Biol. 23, 5354-5365 (2003). (Pubitemid 36950890)
29. Kotaja, N. et al. Preparation, isolation and characterization of stage-specific spermatogenic cells for cellular and molecular analysis. Nat. Methods 1, 249-254 (2004).
30. Zhang, Z. et al. Identification of lysine succinylation as a new post-translational modification. Nat. Chem. Biol. 7, 58-63 (2011).