Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4 - PubMed (original) (raw)
Comparative Study
. 1987 Feb 25;262(6):2854-60.
- PMID: 3818624
Free article
Comparative Study
Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4
M Couppez et al. J Biol Chem. 1987.
Free article
Abstract
The differently acetylated subfractions of histone H4 isolated from cuttlefish testis and from calf thymus were separated by ion exchange chromatography on sulfopropyl-Sephadex, using a shallow linear gradient of guanidine hydrochloride in the presence of 6 M urea at pH 3.0. The tetra-, tri-, di-, mono-, and nonacetylated forms of cuttlefish H4 represent 2, 6.4, 18, 32.2, and 41.4% of the whole histone, respectively. The di-, mono-, and nonacetylated forms of calf H4 represent 11.7, 41.3, and 44% of the whole histone, respectively. The acetylation sites were determined in each subfraction by identification of the acetylated peptides. In each acetylated H4 subfraction, the acetylated tryptic peptides were identified by peptide mapping and amino acid analysis with reference to the peptide map of nonacetylated H4. In cuttlefish testis H4, lysine 12 is the main site of acetylation in the monoacetylated subfraction; lysines 5 and 12 are found acetylated in diacetylated H4; lysines 5, 12, and 16 are found acetylated in triacetylated H4. From these results and the stoichiometry of the different H4 subfractions, it can be concluded that lysine 5 is acetylated after lysine 12. In calf thymus, lysine 16 is the only site of acetylation in the monoacetylated subfraction. All the diacetylated forms are acetylated in lysine 16, the second site of acetylation being, in decreasing order, lysine 12, lysine 5, or lysine 8. These observations suggest that acetylation occurs in a sequential manner. Moreover, the sites of acetylation depend upon the biological event in which acetylation is involved.
Similar articles
- Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. Evidence for functionally distinct H4 acetylation sites.
Chicoine LG, Schulman IG, Richman R, Cook RG, Allis CD. Chicoine LG, et al. J Biol Chem. 1986 Jan 25;261(3):1071-6. J Biol Chem. 1986. PMID: 3080415 - Identification of five sites of acetylation in alfalfa histone H4.
Waterborg JH. Waterborg JH. Biochemistry. 1992 Jul 14;31(27):6211-9. doi: 10.1021/bi00142a006. Biochemistry. 1992. PMID: 1627562 - Amino-terminal sequences and sites of in vivo acetylation of trout-testis histones 3 and IIb 2.
Candido EP, Dixon GH. Candido EP, et al. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2015-9. doi: 10.1073/pnas.69.8.2015. Proc Natl Acad Sci U S A. 1972. PMID: 4506069 Free PMC article. - Specificity of antibodies raised against triacetylated histone H4.
Muller S, Isabey A, Couppez M, Plaue S, Sommermeyer G, Van Regenmortel MH. Muller S, et al. Mol Immunol. 1987 Jul;24(7):779-89. doi: 10.1016/0161-5890(87)90062-9. Mol Immunol. 1987. PMID: 2443844 - Histone acetylation and deacetylation: identification of acetylation and methylation sites of HeLa histone H4 by mass spectrometry.
Zhang K, Williams KE, Huang L, Yau P, Siino JS, Bradbury EM, Jones PR, Minch MJ, Burlingame AL. Zhang K, et al. Mol Cell Proteomics. 2002 Jul;1(7):500-8. doi: 10.1074/mcp.m200031-mcp200. Mol Cell Proteomics. 2002. PMID: 12239278
Cited by
- Histone H4 acetylation and transcription in amphibian chromatin.
Sommerville J, Baird J, Turner BM. Sommerville J, et al. J Cell Biol. 1993 Jan;120(2):277-90. doi: 10.1083/jcb.120.2.277. J Cell Biol. 1993. PMID: 8421048 Free PMC article. - DNA strand breaks alter histone ADP-ribosylation.
Boulikas T. Boulikas T. Proc Natl Acad Sci U S A. 1989 May;86(10):3499-503. doi: 10.1073/pnas.86.10.3499. Proc Natl Acad Sci U S A. 1989. PMID: 2726732 Free PMC article. - Early butyrate induced acetylation of histone H4 is proteoform specific and linked to methylation state.
Wang T, Holt MV, Young NL. Wang T, et al. Epigenetics. 2018;13(5):519-535. doi: 10.1080/15592294.2018.1475979. Epub 2018 Aug 7. Epigenetics. 2018. PMID: 29940793 Free PMC article. - Multivalent nucleosome scaffolding by bromodomain and extraterminal domain tandem bromodomains.
Olp MD, Bursch KL, Wynia-Smith SL, Nuñez R, Goetz CJ, Jackson V, Smith BC. Olp MD, et al. J Biol Chem. 2025 Mar;301(3):108289. doi: 10.1016/j.jbc.2025.108289. Epub 2025 Feb 10. J Biol Chem. 2025. PMID: 39938804 Free PMC article. - Histone hyperacetylation can induce unfolding of the nucleosome core particle.
Oliva R, Bazett-Jones DP, Locklear L, Dixon GH. Oliva R, et al. Nucleic Acids Res. 1990 May 11;18(9):2739-47. doi: 10.1093/nar/18.9.2739. Nucleic Acids Res. 1990. PMID: 2339060 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources