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. 1993 Sep 1;294(Pt 2):557–561. doi: 10.1042/bj2940557

Selective use of H4 acetylation sites in the yeast Saccharomyces cerevisiae.

D J Clarke 1, L P O'Neill 1, B M Turner 1
PMCID: PMC1134491  PMID: 8373369

Abstract

The acetylation of specific lysine residues in the histone H4 may play a role in regulating various genes in the yeast Saccharomyces cerevisiae [Grunstein (1990) Annu. Rev. Cell Biol. 6, 643-678]. The detailed consideration of this possibility has been hampered by the lack of information on the frequency with which different H4 lysine residues are acetylated in yeast. In this paper, we use Western blotting from acid/urea/Triton gels and immunostaining with antisera specific for H4 molecules acetylated at particular lysine residues to show that 70-80% of H4 molecules in S. cerevisiae contain one or more acetylated lysines, and that lysines-5, -8, -12 and -16 are acetylated in an ordered, non-random fashion. The monoacetylated isoform (H4Ac1) is acetylated predominantly at lysine-16 (rarely at lysine-12), H4Ac2 is acetylated at lysine-16 and at either lysine-12 or at -8, while lysine-5 is acetylated frequently only in H4Ac3 and in H4Ac4.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alfageme C. R., Zweidler A., Mahowald A., Cohen L. H. Histones of Drosophila embryos. Electrophoretic isolation and structural studies. J Biol Chem. 1974 Jun 25;249(12):3729–3736. [PubMed] [Google Scholar]
  2. Allegra P., Sterner R., Clayton D. F., Allfrey V. G. Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequences. J Mol Biol. 1987 Jul 20;196(2):379–388. doi: 10.1016/0022-2836(87)90698-x. [DOI] [PubMed] [Google Scholar]
  3. Boffa L. C., Walker J., Chen T. A., Sterner R., Mariani M. R., Allfrey V. G. Factors affecting nucleosome structure in transcriptionally active chromatin. Histone acetylation, nascent RNA and inhibitors of RNA synthesis. Eur J Biochem. 1990 Dec 27;194(3):811–823. doi: 10.1111/j.1432-1033.1990.tb19474.x. [DOI] [PubMed] [Google Scholar]
  4. Chen-Cleland T. A., Smith M. M., Le S., Sternglanz R., Allfrey V. G. Nucleosome structural changes during derepression of silent mating-type loci in yeast. J Biol Chem. 1993 Jan 15;268(2):1118–1124. [PubMed] [Google Scholar]
  5. Chicoine L. G., Schulman I. G., Richman R., Cook R. G., Allis C. D. Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. Evidence for functionally distinct H4 acetylation sites. J Biol Chem. 1986 Jan 25;261(3):1071–1076. [PubMed] [Google Scholar]
  6. Couppez M., Martin-Ponthieu A., Sautière P. Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4. J Biol Chem. 1987 Feb 25;262(6):2854–2860. [PubMed] [Google Scholar]
  7. Davie J. R. Two-dimensional gel systems for rapid histone analysis for use in minislab polyacrylamide gel electrophoresis. Anal Biochem. 1982 Mar 1;120(2):276–281. doi: 10.1016/0003-2697(82)90348-7. [DOI] [PubMed] [Google Scholar]
  8. Grunstein M. Histone function in transcription. Annu Rev Cell Biol. 1990;6:643–678. doi: 10.1146/annurev.cb.06.110190.003235. [DOI] [PubMed] [Google Scholar]
  9. Hebbes T. R., Thorne A. W., Crane-Robinson C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 1988 May;7(5):1395–1402. doi: 10.1002/j.1460-2075.1988.tb02956.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Johnson L. M., Kayne P. S., Kahn E. S., Grunstein M. Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6286–6290. doi: 10.1073/pnas.87.16.6286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kayne P. S., Kim U. J., Han M., Mullen J. R., Yoshizaki F., Grunstein M. Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell. 1988 Oct 7;55(1):27–39. doi: 10.1016/0092-8674(88)90006-2. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. López-Rodas G., Tordera V., Sánchez del Pino M. M., Franco L. Yeast contains multiple forms of histone acetyltransferase. J Biol Chem. 1989 Nov 15;264(32):19028–19033. [PubMed] [Google Scholar]
  14. Megee P. C., Morgan B. A., Mittman B. A., Smith M. M. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science. 1990 Feb 16;247(4944):841–845. doi: 10.1126/science.2106160. [DOI] [PubMed] [Google Scholar]
  15. Munks R. J., Moore J., O'Neill L. P., Turner B. M. Histone H4 acetylation in Drosophila. Frequency of acetylation at different sites defined by immunolabelling with site-specific antibodies. FEBS Lett. 1991 Jun 24;284(2):245–248. doi: 10.1016/0014-5793(91)80695-y. [DOI] [PubMed] [Google Scholar]
  16. Nelson D. A., Alonso W. R. Extraction of histones H2A, H3 and H4 from yeast nuclei. Measurement of the extent of yeast histone acetylation following one-dimensional gel electrophoresis. Biochim Biophys Acta. 1983 Nov 17;741(2):269–271. doi: 10.1016/0167-4781(83)90068-4. [DOI] [PubMed] [Google Scholar]
  17. Nelson D. A. Histone acetylation in baker's yeast. Maintenance of the hyperacetylated configuration in log phase protoplasts. J Biol Chem. 1982 Feb 25;257(4):1565–1568. [PubMed] [Google Scholar]
  18. Park E. C., Szostak J. W. Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML. Mol Cell Biol. 1990 Sep;10(9):4932–4934. doi: 10.1128/mcb.10.9.4932. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ridsdale J. A., Davie J. R. Chicken erythrocyte polynucleosomes which are soluble at physiological ionic strength and contain linker histones are highly enriched in beta-globin gene sequences. Nucleic Acids Res. 1987 Feb 11;15(3):1081–1096. doi: 10.1093/nar/15.3.1081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sommerville J., Baird J., Turner B. M. Histone H4 acetylation and transcription in amphibian chromatin. J Cell Biol. 1993 Jan;120(2):277–290. doi: 10.1083/jcb.120.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Thorne A. W., Kmiciek D., Mitchelson K., Sautiere P., Crane-Robinson C. Patterns of histone acetylation. Eur J Biochem. 1990 Nov 13;193(3):701–713. doi: 10.1111/j.1432-1033.1990.tb19390.x. [DOI] [PubMed] [Google Scholar]
  22. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Turner B. M., Birley A. J., Lavender J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell. 1992 Apr 17;69(2):375–384. doi: 10.1016/0092-8674(92)90417-b. [DOI] [PubMed] [Google Scholar]
  24. Turner B. M., Fellows G. Specific antibodies reveal ordered and cell-cycle-related use of histone-H4 acetylation sites in mammalian cells. Eur J Biochem. 1989 Jan 15;179(1):131–139. doi: 10.1111/j.1432-1033.1989.tb14530.x. [DOI] [PubMed] [Google Scholar]
  25. Turner B. M. Histone acetylation and control of gene expression. J Cell Sci. 1991 May;99(Pt 1):13–20. doi: 10.1242/jcs.99.1.13. [DOI] [PubMed] [Google Scholar]
  26. Turner B. M., O'Neill L. P., Allan I. M. Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies. FEBS Lett. 1989 Aug 14;253(1-2):141–145. doi: 10.1016/0014-5793(89)80947-0. [DOI] [PubMed] [Google Scholar]
  27. Vu Q. A., Zhang D. E., Chroneos Z. C., Nelson D. A. Polyamines inhibit the yeast histone deacetylase. FEBS Lett. 1987 Aug 10;220(1):79–83. doi: 10.1016/0014-5793(87)80879-7. [DOI] [PubMed] [Google Scholar]
  28. Wu R. S., Panusz H. T., Hatch C. L., Bonner W. M. Histones and their modifications. CRC Crit Rev Biochem. 1986;20(2):201–263. doi: 10.3109/10409238609083735. [DOI] [PubMed] [Google Scholar]

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