Abstract
We have developed a method for partially purifying chromatin from Saccharomyces cerevisiae (baker's yeast) to a level suitable for studies of its higher-order folding. This has required the use of yeast strains that are free of the ubiquitous yeast "killer" virus. Results from dynamic light scattering, electron microscopy, and x-ray diffraction show that the yeast chromatin undergoes a cation-dependent folding into 30-nm filaments that resemble those characteristic of higher-cell chromatin; moreover, the packing of nucleosomes within the yeast 30-nm filaments is similar to that of higher cells. These results imply that yeast has a protein or protein domain that serves the role of the histone H 1 found in higher cells; physical and genetic studies of the yeast activity could help elucidate the structure and function of H 1. Images of the yeast 30-nm filaments can be used to test crossed-linker models for 30-nm filament structure.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Allan J., Rau D. C., Harborne N., Gould H. Higher order structure in a short repeat length chromatin. J Cell Biol. 1984 Apr;98(4):1320–1327. doi: 10.1083/jcb.98.4.1320. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bates D. L., Thomas J. O. Histones H1 and H5: one or two molecules per nucleosome? Nucleic Acids Res. 1981 Nov 25;9(22):5883–5894. doi: 10.1093/nar/9.22.5883. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Butler P. J., Thomas J. O. Changes in chromatin folding in solution. J Mol Biol. 1980 Jul 15;140(4):505–529. doi: 10.1016/0022-2836(80)90268-5. [DOI] [PubMed] [Google Scholar]
- Certa U., Colavito-Shepanski M., Grunstein M. Yeast may not contain histone H1: the only known 'histone H1-like' protein in Saccharomyces cerevisiae is a mitochondrial protein. Nucleic Acids Res. 1984 Nov 12;12(21):7975–7985. doi: 10.1093/nar/12.21.7975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elliott S. G., McLaughlin C. S. Synthesis and modification of proteins during the cell cycle of the yeast Saccharomyces cerevisiae. J Bacteriol. 1979 Mar;137(3):1185–1190. doi: 10.1128/jb.137.3.1185-1190.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Finch J. T., Klug A. Solenoidal model for superstructure in chromatin. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1897–1901. doi: 10.1073/pnas.73.6.1897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Graziano V., Gerchman S. E., Ramakrishnan V. Reconstitution of chromatin higher-order structure from histone H5 and depleted chromatin. J Mol Biol. 1988 Oct 20;203(4):997–1007. doi: 10.1016/0022-2836(88)90124-6. [DOI] [PubMed] [Google Scholar]
- Lohr D. The salt dependence of chicken and yeast chromatin structure. Effects on internucleosomal organization and relation to active chromatin. J Biol Chem. 1986 Jul 25;261(21):9904–9914. [PubMed] [Google Scholar]
- Marion C., Hesse-Bezot C., Bezot P., Marion M. J., Roux B., Bernengo J. C. The effect of histone H1 on the compaction of oligonucleosomes. A quasielastic light scattering study. Biophys Chem. 1985 Jun;22(1-2):53–64. doi: 10.1016/0301-4622(85)80025-9. [DOI] [PubMed] [Google Scholar]
- Pearson E. C., Butler P. J., Thomas J. O. Higher-order structure of nucleosome oligomers from short-repeat chromatin. EMBO J. 1983;2(8):1367–1372. doi: 10.1002/j.1460-2075.1983.tb01593.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rattner J. B., Saunders C., Davie J. R., Hamkalo B. A. Ultrastructural organization of yeast chromatin. J Cell Biol. 1982 Apr;93(1):217–222. doi: 10.1083/jcb.93.1.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Richmond T. J., Finch J. T., Rushton B., Rhodes D., Klug A. Structure of the nucleosome core particle at 7 A resolution. Nature. 1984 Oct 11;311(5986):532–537. doi: 10.1038/311532a0. [DOI] [PubMed] [Google Scholar]
- Thomas J. O., Furber V. Yeast chromatin structure. FEBS Lett. 1976 Jul 15;66(2):274–280. doi: 10.1016/0014-5793(76)80521-2. [DOI] [PubMed] [Google Scholar]
- Vodkin M. Induction of yeast killer factor mutations. J Bacteriol. 1977 Oct;132(1):346–348. doi: 10.1128/jb.132.1.346-348.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wells D., McBride C. A comprehensive compilation and alignment of histones and histone genes. Nucleic Acids Res. 1989;17 (Suppl):r311–r346. doi: 10.1093/nar/17.suppl.r311. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Widom J., Finch J. T., Thomas J. O. Higher-order structure of long repeat chromatin. EMBO J. 1985 Dec 1;4(12):3189–3194. doi: 10.1002/j.1460-2075.1985.tb04064.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Widom J., Klug A. Structure of the 300A chromatin filament: X-ray diffraction from oriented samples. Cell. 1985 Nov;43(1):207–213. doi: 10.1016/0092-8674(85)90025-x. [DOI] [PubMed] [Google Scholar]
- Widom J. Physicochemical studies of the folding of the 100 A nucleosome filament into the 300 A filament. Cation dependence. J Mol Biol. 1986 Aug 5;190(3):411–424. doi: 10.1016/0022-2836(86)90012-4. [DOI] [PubMed] [Google Scholar]
- Widom J. Toward a unified model of chromatin folding. Annu Rev Biophys Biophys Chem. 1989;18:365–395. doi: 10.1146/annurev.bb.18.060189.002053. [DOI] [PubMed] [Google Scholar]
- Williams S. P., Athey B. D., Muglia L. J., Schappe R. S., Gough A. H., Langmore J. P. Chromatin fibers are left-handed double helices with diameter and mass per unit length that depend on linker length. Biophys J. 1986 Jan;49(1):233–248. doi: 10.1016/S0006-3495(86)83637-2. [DOI] [PMC free article] [PubMed] [Google Scholar]