Abstract
The four core histones (H2a, H2b, H3, and H4) bound to simian virus 40 minichromosomes isolated from infected cells contain rapidly labeled acetyl groups in internal positions of the histone polypeptide chain. Upon chase, these acetyl residues decay with a half-life of less than 15 min. The acetyl groups are incorporated in histones bound to mature chromosomes and not in newly synthesized histones bound to replicating viral chromosomes. The rate of acetate incorporation is not related to the degree of steady state acetylation of the individual viral or cellular histones. This rate is 4-fold higher for the viral chromatin than for its cellular counterpart isolated from the same nuclei. The possible role for histone acetylation in viral genome expression is discussed.
Full text
PDF




Images in this article
Selected 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]
- 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]
- Bellard M., Oudet P., Germond J. E., Chambon P. Subunit structure of simian-virus-40 minichromosome. Eur J Biochem. 1976 Nov 15;70(2):543–553. doi: 10.1111/j.1432-1033.1976.tb11046.x. [DOI] [PubMed] [Google Scholar]
- Christiansen G., Griffith J. Salt and divalent cations affect the flexible nature of the natural beaded chromatin structure. Nucleic Acids Res. 1977 Jun;4(6):1837–1851. doi: 10.1093/nar/4.6.1837. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Crawford L. V., Cole C. N., Smith A. E., Paucha E., Tegtmeyer P., Rundell K., Berg P. Organization and expression of early genes of simian virus 40. Proc Natl Acad Sci U S A. 1978 Jan;75(1):117–121. doi: 10.1073/pnas.75.1.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cremisi C., Pignatti P. F., Croissant O., Yaniv M. Chromatin-like structures in polyoma virus and simian virus 10 lytic cycle. J Virol. 1975 Jan;17(1):204–211. doi: 10.1128/jvi.17.1.204-211.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Crémisi C., Chestier A., Yaniv M. Assembly of SV40 and polyoma minichromosomes during replication. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 1):409–416. doi: 10.1101/sqb.1978.042.01.043. [DOI] [PubMed] [Google Scholar]
- Crémisi C., Chestier A., Yaniv M. Preferential association of newly synthesized histones with replicating SV40 DNA. Cell. 1977 Dec;12(4):947–951. doi: 10.1016/0092-8674(77)90159-3. [DOI] [PubMed] [Google Scholar]
- DeLange R. J., Smith E. L. Histones: structure and function. Annu Rev Biochem. 1971;40:279–314. doi: 10.1146/annurev.bi.40.070171.001431. [DOI] [PubMed] [Google Scholar]
- Elgin S. C., Weintraub H. Chromosomal proteins and chromatin structure. Annu Rev Biochem. 1975;44:725–774. doi: 10.1146/annurev.bi.44.070175.003453. [DOI] [PubMed] [Google Scholar]
- Fareed G. C., Davoli D. Molecular biology of papovaviruses. Annu Rev Biochem. 1977;46:471–522. doi: 10.1146/annurev.bi.46.070177.002351. [DOI] [PubMed] [Google Scholar]
- Felsenfeld G. Chromatin. Nature. 1978 Jan 12;271(5641):115–122. doi: 10.1038/271115a0. [DOI] [PubMed] [Google Scholar]
- Foe V. E. Modulation of ribosomal RNA synthesis in Oncopeltus fasciatus: an electron microscopic study of the relationship between changes in chromatin structure and transcriptional activity. Cold Spring Harb Symp Quant Biol. 1978;42(Pt 2):723–740. doi: 10.1101/sqb.1978.042.01.074. [DOI] [PubMed] [Google Scholar]
- Germond J. E., Hirt B., Oudet P., Gross-Bellark M., Chambon P. Folding of the DNA double helix in chromatin-like structures from simian virus 40. Proc Natl Acad Sci U S A. 1975 May;72(5):1843–1847. doi: 10.1073/pnas.72.5.1843. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Green M. H., Brooks T. L. The sv40 transcription complex. II. Non-dissociation of protein from SV40 chromatin during transcription. Nucleic Acids Res. 1977 Dec;4(12):4279–4289. doi: 10.1093/nar/4.12.4279. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Griffith J. D. Chromatin structure: deduced from a minichromosome. Science. 1975 Mar 28;187(4182):1202–1203. doi: 10.1126/science.187.4182.1202. [DOI] [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]
- Jackson V., Shires A., Tanphaichitr N., Chalkley R. Modifications to histones immediately after synthesis. J Mol Biol. 1976 Jun 25;104(2):471–483. doi: 10.1016/0022-2836(76)90282-5. [DOI] [PubMed] [Google Scholar]
- 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]
- Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
- Louie A. J., Candido E. P., Dixon G. H. Enzymatic modifications and their possible roles in regulating the binding of basic proteins to DNA and in controlling chromosomal structure. Cold Spring Harb Symp Quant Biol. 1974;38:803–819. doi: 10.1101/sqb.1974.038.01.084. [DOI] [PubMed] [Google Scholar]
- Louie A. J. The organization of proteins in polyoma and cellular chromatin. Cold Spring Harb Symp Quant Biol. 1975;39(Pt 1):259–266. doi: 10.1101/sqb.1974.039.01.034. [DOI] [PubMed] [Google Scholar]
- Pogo B. G., Pogo A. O., Allfrey V. G., Mirsky A. E. Changing patterns of histone acetylation and RNA synthesis in regeneration of the liver. Proc Natl Acad Sci U S A. 1968 Apr;59(4):1337–1344. doi: 10.1073/pnas.59.4.1337. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Prives C., Gilboa E., Revel M., Winocour E. Cell-free translation of simian virus 40 early messenger RNA coding for viral T-antigen. Proc Natl Acad Sci U S A. 1977 Feb;74(2):457–461. doi: 10.1073/pnas.74.2.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Riggs M. G., Whittaker R. G., Neumann J. R., Ingram V. M. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature. 1977 Aug 4;268(5619):462–464. doi: 10.1038/268462a0. [DOI] [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]
- Schaffhausen B. S., Benjamin T. L. Deficiency in histone acetylation in nontransforming host range mutants of polyoma virus. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1092–1096. doi: 10.1073/pnas.73.4.1092. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schaffhausen B. S., Silver J. E., Benjamin T. L. Tumor antigen(s) in cell productively infected by wild-type polyoma virus and mutant NG-18. Proc Natl Acad Sci U S A. 1978 Jan;75(1):79–83. doi: 10.1073/pnas.75.1.79. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Silver J., Schaffhausen B., Benjamin T. Tumor antigens induced by nontransforming mutants of polyoma virus. Cell. 1978 Oct;15(2):485–496. doi: 10.1016/0092-8674(78)90018-1. [DOI] [PubMed] [Google Scholar]
- Varshavsky A. J., Bakayev V. V., Chumackov P. M., Georgiev G. P. Minichromosome of simian virus 40: presence of histone HI. Nucleic Acids Res. 1976 Aug;3(8):2101–2113. doi: 10.1093/nar/3.8.2101. [DOI] [PMC free article] [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]
- 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]
- Yamamoto K. R., Alberts B. M. Steroid receptors: elements for modulation of eukaryotic transcription. Annu Rev Biochem. 1976;45:721–746. doi: 10.1146/annurev.bi.45.070176.003445. [DOI] [PubMed] [Google Scholar]