Skip to main content
PMC home page
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1990 Sep;10(9):4932–4934. doi: 10.1128/mcb.10.9.4932

Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML.

E C Park 1, J W Szostak 1
PMCID: PMC361112  PMID: 2117703

Abstract

The N-terminal serine and four conserved lysine residues near the N-terminus of yeast histone H4 are acetylated. We found that a mutation that changed the fourth lysine to alanine resulted in specific derepression of the silent mating type locus HML, while mutations that altered the N-terminal serine or the first three lysines had only minor phenotypic effects. Our results support an active role for histone H4 in the silencing of gene expression at this locus.

Full text

PDF
4932

Images in this article

4933Image
on p.4933

Selected References

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

  1. Arfin S. M., Bradshaw R. A. Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry. 1988 Oct 18;27(21):7979–7984. doi: 10.1021/bi00421a001. [DOI] [PubMed] [Google Scholar]
  2. Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 1986 Oct 10;234(4773):179–186. doi: 10.1126/science.3018930. [DOI] [PubMed] [Google Scholar]
  3. Boeke J. D., LaCroute F., Fink G. R. A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol Gen Genet. 1984;197(2):345–346. doi: 10.1007/BF00330984. [DOI] [PubMed] [Google Scholar]
  4. Brandt W. F., Patterson K., von Holt C. The histones of yeast. The isolation and partial structure of the core histones. Eur J Biochem. 1980 Sep;110(1):67–76. doi: 10.1111/j.1432-1033.1980.tb04841.x. [DOI] [PubMed] [Google Scholar]
  5. Candido E. P., Reeves R., Davie J. R. Sodium butyrate inhibits histone deacetylation in cultured cells. Cell. 1978 May;14(1):105–113. doi: 10.1016/0092-8674(78)90305-7. [DOI] [PubMed] [Google Scholar]
  6. Clark-Adams C. D., Norris D., Osley M. A., Fassler J. S., Winston F. Changes in histone gene dosage alter transcription in yeast. Genes Dev. 1988 Feb;2(2):150–159. doi: 10.1101/gad.2.2.150. [DOI] [PubMed] [Google Scholar]
  7. Davie J. R., Saunders C. A., Walsh J. M., Weber S. C. Histone modifications in the yeast S. Cerevisiae. Nucleic Acids Res. 1981 Jul 10;9(13):3205–3216. doi: 10.1093/nar/9.13.3205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dutcher S. K., Hartwell L. H. The role of S. cerevisiae cell division cycle genes in nuclear fusion. Genetics. 1982 Feb;100(2):175–184. doi: 10.1093/genetics/100.2.175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gonda D. K., Bachmair A., Wünning I., Tobias J. W., Lane W. S., Varshavsky A. Universality and structure of the N-end rule. J Biol Chem. 1989 Oct 5;264(28):16700–16712. [PubMed] [Google Scholar]
  10. 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]
  11. Huang S., Elliott R. C., Liu P. S., Koduri R. K., Weickmann J. L., Lee J. H., Blair L. C., Ghosh-Dastidar P., Bradshaw R. A., Bryan K. M. Specificity of cotranslational amino-terminal processing of proteins in yeast. Biochemistry. 1987 Dec 15;26(25):8242–8246. doi: 10.1021/bi00399a033. [DOI] [PubMed] [Google Scholar]
  12. Isenberg I. Histones. Annu Rev Biochem. 1979;48:159–191. doi: 10.1146/annurev.bi.48.070179.001111. [DOI] [PubMed] [Google Scholar]
  13. Ivy J. M., Klar A. J., Hicks J. B. Cloning and characterization of four SIR genes of Saccharomyces cerevisiae. Mol Cell Biol. 1986 Feb;6(2):688–702. doi: 10.1128/mcb.6.2.688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kanungo M. S., Thakur M. K. Modulation of acetylation of histones and transcription of chromatin by butyric acid and 17beta-estradiol in the brain of rats of various ages. Biochem Biophys Res Commun. 1979 Mar 15;87(1):266–271. doi: 10.1016/0006-291x(79)91675-9. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Kunkel T. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci U S A. 1985 Jan;82(2):488–492. doi: 10.1073/pnas.82.2.488. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Leder A., Leder P. Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells. Cell. 1975 Jul;5(3):319–322. doi: 10.1016/0092-8674(75)90107-5. [DOI] [PubMed] [Google Scholar]
  18. Mathis D. J., Oudet P., Wasylyk B., Chambon P. Effect of histone acetylation on structure and in vitro transcription of chromatin. Nucleic Acids Res. 1978 Oct;5(10):3523–3547. doi: 10.1093/nar/5.10.3523. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Mullen J. R., Kayne P. S., Moerschell R. P., Tsunasawa S., Gribskov M., Colavito-Shepanski M., Grunstein M., Sherman F., Sternglanz R. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J. 1989 Jul;8(7):2067–2075. doi: 10.1002/j.1460-2075.1989.tb03615.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Muller S., Erard M., Burggraf E., Couppez M., Sautière P., Champagne M., Van Regenmortel M. H. Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation. EMBO J. 1982;1(8):939–944. doi: 10.1002/j.1460-2075.1982.tb01275.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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]
  23. Reczek P. R., Weissman D., Hüvös P. E., Fasman G. D. Sodium butyrate induced structural changes in HeLa cell chromatin. Biochemistry. 1982 Mar 2;21(5):993–1002. doi: 10.1021/bi00534a026. [DOI] [PubMed] [Google Scholar]
  24. Smith M. M., Stirling V. B. Histone H3 and H4 gene deletions in Saccharomyces cerevisiae. J Cell Biol. 1988 Mar;106(3):557–566. doi: 10.1083/jcb.106.3.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Tsunasawa S., Stewart J. W., Sherman F. Amino-terminal processing of mutant forms of yeast iso-1-cytochrome c. The specificities of methionine aminopeptidase and acetyltransferase. J Biol Chem. 1985 May 10;260(9):5382–5391. [PubMed] [Google Scholar]
  26. Whiteway M., Freedman R., Van Arsdell S., Szostak J. W., Thorner J. The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus. Mol Cell Biol. 1987 Oct;7(10):3713–3722. doi: 10.1128/mcb.7.10.3713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Whiteway M., Szostak J. W. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell. 1985 Dec;43(2 Pt 1):483–492. doi: 10.1016/0092-8674(85)90178-3. [DOI] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES