Abstract
The ability of calf thymus chromatin to support DNA-dependent RNA synthesis is markedly increased by modification of the histones with acetic anhydride. The extent of chemical acetylation of histones H2a, H2b, H3, and H4 required for the increase of template activity of the chromatin is within that which can be achieved enzymatically in the cell. The evidence suggests that the acetylation of histone side chains stimulates the rate of chain elongation during transcription of chromatin.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- ALLFREY V. G., FAULKNER R., MIRSKY A. E. ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS. Proc Natl Acad Sci U S A. 1964 May;51:786–794. doi: 10.1073/pnas.51.5.786. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bautz E. K., Bautz F. A. Initiation of RNA synthesis: the function of sigma in the binding of RNA polymerase to promoter sites. Nature. 1970 Jun 27;226(5252):1219–1222. doi: 10.1038/2261219a0. [DOI] [PubMed] [Google Scholar]
- Candido E. P., Dixon G. H. Amino-terminal sequences and sites of in vivo acetylation of trout-testis histones 3 and IIb 2 . Proc Natl Acad Sci U S A. 1972 Aug;69(8):2015–2019. doi: 10.1073/pnas.69.8.2015. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Candido E. P., Dixon G. H. Sites of in vivo acetylation in trout testis histone IV. J Biol Chem. 1971 May 25;246(10):3182–3188. [PubMed] [Google Scholar]
- Candido E. P., Dixon G. H. Trout testis cells. 3. Acetylation of histones in different cell types from developing trout testis. J Biol Chem. 1972 Sep 10;247(17):5506–5510. [PubMed] [Google Scholar]
- DeLange R. J., Fambrough D. M., Smith E. L., Bonner J. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. J Biol Chem. 1969 Jan 25;244(2):319–334. [PubMed] [Google Scholar]
- DeLange R. J., Hooper J. A., Smith E. L. Complete amino-acid sequence of calf-thymus histone 3. Proc Natl Acad Sci U S A. 1972 Apr;69(4):882–884. doi: 10.1073/pnas.69.4.882. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gershey E. L., Vidali G., Allfrey V. G. Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J Biol Chem. 1968 Oct 10;243(19):5018–5022. [PubMed] [Google Scholar]
- Gottesfeld J. M., Garrard W. T., Bagi G., Wilson R. F., Bonner J. Partial purification of the template-active fraction of chromatin: a preliminary report. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2193–2197. doi: 10.1073/pnas.71.6.2193. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUANG R. C., BONNER J. Histone, a suppressor of chromosomal RNA synthesis. Proc Natl Acad Sci U S A. 1962 Jul 15;48:1216–1222. doi: 10.1073/pnas.48.7.1216. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jackson V., Shires A., Chalkley R., Granner D. K. Studies on highly metabolically active acetylation and phosphorylation of histones. J Biol Chem. 1975 Jul 10;250(13):4856–4863. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Marushige K., Bonner J. Fractionation of liver chromatin. Proc Natl Acad Sci U S A. 1971 Dec;68(12):2941–2944. doi: 10.1073/pnas.68.12.2941. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marushige K., Bonner J. Template properties of liver chromatin. J Mol Biol. 1966 Jan;15(1):160–174. doi: 10.1016/s0022-2836(66)80218-8. [DOI] [PubMed] [Google Scholar]
- Marushige K., Marushige Y., Wong T. K. Complete displacement of somatic histones during transformation of spermatid chromatin: a model experiment. Biochemistry. 1976 May 18;15(10):2047–2053. doi: 10.1021/bi00655a004. [DOI] [PubMed] [Google Scholar]
- Millette R. L., Trotter C. D. Initiation and release of RNA by DNA-dependent RNA polymerase. Proc Natl Acad Sci U S A. 1970 Jul;66(3):701–708. doi: 10.1073/pnas.66.3.701. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peter E., Candido M., Dixon G. H. Acetylation of trout testis histones in vivo. Site of the modification in histone IIb 1 . J Biol Chem. 1972 Jun 25;247(12):3868–3873. [PubMed] [Google Scholar]
- Ruiz-Carrillo A., Wangh L. J., Allfrey V. G. Processing of newly synthesized histone molecules. Science. 1975 Oct 10;190(4210):117–128. doi: 10.1126/science.1166303. [DOI] [PubMed] [Google Scholar]
- Sanders L. A., Schechter N. M., McCarty K. S. A comparative study of histone acetylation, histone deacetylation, and ribonucleic acid synthesis in avian reticulocytes and erythrocytes. Biochemistry. 1973 Feb 27;12(5):783–791. doi: 10.1021/bi00729a001. [DOI] [PubMed] [Google Scholar]
- Sippel A. E., Hartmann G. R. Rifampicin resistance of RNA polymerase in the binary complex with DNA. Eur J Biochem. 1970 Sep;16(1):152–157. doi: 10.1111/j.1432-1033.1970.tb01066.x. [DOI] [PubMed] [Google Scholar]
- Smart J. E., Bonner J. Studies on the role of histones in relation to the template activity and precipitability of chromatin at physiological ionic strengths. J Mol Biol. 1971 Jun 28;58(3):675–684. doi: 10.1016/0022-2836(71)90032-5. [DOI] [PubMed] [Google Scholar]
- Vidali G., Gershey E. L., Allfrey V. G. Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. J Biol Chem. 1968 Dec 25;243(24):6361–6366. [PubMed] [Google Scholar]
- Wong T. K., Marushige K. Modification of histone binding in calf thymus chromatin and in the chromatin-protamine complex by acetic anhydride. Biochemistry. 1976 May 18;15(10):2041–2046. doi: 10.1021/bi00655a003. [DOI] [PubMed] [Google Scholar]
- Wong T. K., Marushige K. Modification of histone binding in calf thymus chromatin by protamine. Biochemistry. 1975 Jan 14;14(1):122–127. doi: 10.1021/bi00672a021. [DOI] [PubMed] [Google Scholar]