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. 1979;6(5):1909–1927. doi: 10.1093/nar/6.5.1909

Comparison on the structure and transcriptional capability of growing phase and stationary yeast chromatin: a model for reversible gene activation.

D Lohr, G Ide
PMCID: PMC327820  PMID: 377235

Abstract

We have compared the structure of intra-nuclear and isolated chromatin from logarithmically growing yeast cells to chromatin from cells which had entered the stationary phase and ceased growing. Both chromatins show a similar nucleosomal repeat pattern, 160 bp repeat size, with staphylococcal nuclease and similar variability in repeat sizes within the genome. DNase I produces the same ladder (less than 120 b) and a quite similar extended ladder (120-300 b) which shows that both chromatins have phased nucleosomes. However, the rate of DNase I digestion of growing phase is greater than in stationary. Functionally speaking, growing phase nuclei are 5-20 times as active in the rate of endogenous transcription (all three polymerases are involved). The transcriptional and DNase I susceptibility differences noted in nuclei are maintained in sucrose gradient isolated oligonucleosomes and mononucleosomes from the two states.

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Selected References

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  1. Adman R., Schultz L. D., Hall B. D. Transcription in yeast: separation and properties of multiple FNA polymerases. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1702–1706. doi: 10.1073/pnas.69.7.1702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Axel R. Cleavage of DNA in nuclei and chromatin with staphylococcal nuclease. Biochemistry. 1975 Jul;14(13):2921–2925. doi: 10.1021/bi00684a020. [DOI] [PubMed] [Google Scholar]
  3. Bellard M., Gannon F., Chambon P. Nucleosome structure III: the structure and transcriptional activity of the chromatin containing the ovalbumin and globin genes in chick oviduct nuclei. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 2):779–791. doi: 10.1101/sqb.1978.042.01.078. [DOI] [PubMed] [Google Scholar]
  4. Camerini-Otero R. D., Sollner-Webb B., Simon R. H., Williamson P., Zasloff M., Felsenfeld G. Nucleosome structure, DNA folding, and gene activity. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 1):57–75. doi: 10.1101/sqb.1978.042.01.008. [DOI] [PubMed] [Google Scholar]
  5. Felsenfeld G. Chromatin. Nature. 1978 Jan 12;271(5641):115–122. doi: 10.1038/271115a0. [DOI] [PubMed] [Google Scholar]
  6. Frank K. R., Mills D. Ribosome activity and degradation in meiotic cells of Saccharomyces cerevisiae. Mol Gen Genet. 1978 Mar 20;160(1):59–65. doi: 10.1007/BF00275119. [DOI] [PubMed] [Google Scholar]
  7. Garel A., Axel R. Selective digestion of transcriptionally active ovalbumin genes from oviduct nuclei. Proc Natl Acad Sci U S A. 1976 Nov;73(11):3966–3970. doi: 10.1073/pnas.73.11.3966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gottesfeld J. M., Butler P. J. Structure of transcriptionally-active chromatin subunits. Nucleic Acids Res. 1977 Sep;4(9):3155–3173. doi: 10.1093/nar/4.9.3155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hereford L. M., Rosbash M. Number and distribution of polyadenylated RNA sequences in yeast. Cell. 1977 Mar;10(3):453–462. doi: 10.1016/0092-8674(77)90032-0. [DOI] [PubMed] [Google Scholar]
  10. Kornberg R. D. Structure of chromatin. Annu Rev Biochem. 1977;46:931–954. doi: 10.1146/annurev.bi.46.070177.004435. [DOI] [PubMed] [Google Scholar]
  11. Lacy E., Axel R. Analysis of DNA of isolated chromatin subunits. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3978–3982. doi: 10.1073/pnas.72.10.3978. [DOI] [PMC free article] [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. Lohr D., Corden J., Tatchell K., Kovacic R. T., Van Holde K. E. Comparative subunit structure of HeLa, yeast, and chicken erythrocyte chromatin. Proc Natl Acad Sci U S A. 1977 Jan;74(1):79–83. doi: 10.1073/pnas.74.1.79. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lohr D., Kovacic R. T., Van Holde K. E. Quantitative analysis of the digestion of yeast chromatin by staphylococcal nuclease. Biochemistry. 1977 Feb 8;16(3):463–471. doi: 10.1021/bi00622a020. [DOI] [PubMed] [Google Scholar]
  15. Lohr D., Tatchell K., Van Holde K. E. On the occurrence of nucleosome phasing in chromatin. Cell. 1977 Nov;12(3):829–836. doi: 10.1016/0092-8674(77)90281-1. [DOI] [PubMed] [Google Scholar]
  16. Maniatis T., Jeffrey A., van deSande H. Chain length determination of small double- and single-stranded DNA molecules by polyacrylamide gel electrophoresis. Biochemistry. 1975 Aug 26;14(17):3787–3794. doi: 10.1021/bi00688a010. [DOI] [PubMed] [Google Scholar]
  17. McMaster-Kaye R., Kaye J. S. Staining of histones on polyacrylamide gels with amido black and fast green. Anal Biochem. 1974 Sep;61(1):120–132. doi: 10.1016/0003-2697(74)90339-x. [DOI] [PubMed] [Google Scholar]
  18. Nelson D. A., Beltz W. R., Rill R. L. Chromatin subunits from baker's yeast: isolation and partial characterization. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1343–1347. doi: 10.1073/pnas.74.4.1343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Prunell A., Kornberg R. D. Relation of nucleosomes to DNA sequences. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 1):103–108. doi: 10.1101/sqb.1978.042.01.011. [DOI] [PubMed] [Google Scholar]
  20. Riley D., Weintraub H. Nucleosomal DNA is digested to repeats of 10 bases by exonuclease III. Cell. 1978 Feb;13(2):281–293. doi: 10.1016/0092-8674(78)90197-6. [DOI] [PubMed] [Google Scholar]
  21. Roeder R. G. Multiple forms of deoxyribonucleic acid-dependent ribonucleic acid polymerase in Xenopus laevis. Isolation and partial characterization. J Biol Chem. 1974 Jan 10;249(1):241–248. [PubMed] [Google Scholar]
  22. Scheer U. Changes of nucleosome frequency in nucleolar and non-nucleolar chromatin as a function of transcription: an electron microscopic study. Cell. 1978 Mar;13(3):535–549. doi: 10.1016/0092-8674(78)90327-6. [DOI] [PubMed] [Google Scholar]
  23. Schultz L. D., Hall B. D. Transcription in yeast: alpha-amanitin sensitivity and other properties which distinguish between RNA polymerases I and III. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1029–1033. doi: 10.1073/pnas.73.4.1029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Schultz L. D. Transcriptional role of yeast deoxyribonucleic acid dependent ribonucleic acid polymerase III. Biochemistry. 1978 Feb 21;17(4):750–758. doi: 10.1021/bi00597a031. [DOI] [PubMed] [Google Scholar]
  25. Sollner-Webb B., Felsenfeld G. A comparison of the digestion of nuclei and chromatin by staphylococcal nuclease. Biochemistry. 1975 Jul;14(13):2915–2920. doi: 10.1021/bi00684a019. [DOI] [PubMed] [Google Scholar]
  26. Tata J. R., Baker B. Enzymatic fractionation of nuclei: polynucleosomes and RNA polymerase II as endogenous transcriptional complexes. J Mol Biol. 1978 Jan 25;118(3):249–272. doi: 10.1016/0022-2836(78)90227-9. [DOI] [PubMed] [Google Scholar]
  27. Tatchell K., Van Holde K. E. Compact oligomers and nucleosome phasing. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3583–3587. doi: 10.1073/pnas.75.8.3583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Valenzuela P., Hager G. L., Weinberg F., Rutter W. J. Molecular structure of yeast RNA polymerase III: demonstration of the tripartite transcriptive system in lower eukaryotes. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1024–1028. doi: 10.1073/pnas.73.4.1024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Weintraub H., Groudine M. Chromosomal subunits in active genes have an altered conformation. Science. 1976 Sep 3;193(4256):848–856. doi: 10.1126/science.948749. [DOI] [PubMed] [Google Scholar]

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