Abstract
Thyrotropin (TSH) increases the labeling of histones of H1 and H3 in thyroid slices incubated with 32Pi. We have prepared nuclei from control and TSH-treated thyroid slices, digested them with micrococcal nuclease, and extracted specific populations of nucleosomes by salt fractionation. Mononucleosomes, derived from the most nuclease-sensitive regions of chromatin, appeared to be selectively enriched in 32P-labeled H1 and H3. However, we were able to detect TSH enhancement of H1 and H3 labeling only in nucleosome multimers derived from less nuclease-sensitive chromatin. Recent studies have indicated that transcriptionally competent regions of chromatin may be more susceptible to micrococcal nuclease digestion than inactive regions. Our results therefore suggest that H1 and H3 may be actively phosphorylated in transcriptionally competent chromatin; however, they suggest either that hormone-dependent phosphorylation of H1 and/or H3 does not confer transcriptional competence, or that not all transcriptionally competent chromatin is nuclease sensitive.
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- Adler A. J., Schaffhausen B., Langan T. A., Fasman G. D. Altered conformational effects of phosphorylated lysine-rich histone (f-1) in f-1--deoxyribonucleic acid complexes. Circular dichroism and immunological studies. Biochemistry. 1971 Mar 2;10(5):909–913. doi: 10.1021/bi00781a028. [DOI] [PubMed] [Google Scholar]
- Allan J., Hartman P. G., Crane-Robinson C., Aviles F. X. The structure of histone H1 and its location in chromatin. Nature. 1980 Dec 25;288(5792):675–679. doi: 10.1038/288675a0. [DOI] [PubMed] [Google Scholar]
- Allis C. D., Glover C. V., Gorovsky M. A. Micronuclei of Tetrahymena contain two types of histone H3. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4857–4861. doi: 10.1073/pnas.76.10.4857. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Aström S., von der Decken A. Release of transcriptionally active chromatin from liver nuclei by micrococcus nuclease. Life Sci. 1980 Mar 10;26(10):797–804. doi: 10.1016/0024-3205(80)90286-6. [DOI] [PubMed] [Google Scholar]
- Bloom K. S., Anderson J. N. Fractionation of hen oviduct chromatin into transcriptionally active and inactive regions after selective micrococcal nuclease digestion. Cell. 1978 Sep;15(1):141–150. doi: 10.1016/0092-8674(78)90090-9. [DOI] [PubMed] [Google Scholar]
- Dimitriadis G. J., Tata J. R. Subnuclear fractionation by mild micrococcal-nuclease treatment of nuclei of different transcriptional activities causes a partition of expressed and non-expressed genes. Biochem J. 1980 May 1;187(2):467–477. doi: 10.1042/bj1870467. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fasy T. M., Inoue A., Johnson E. M., Allfrey V. G. Phosphorlyation of H1 and H5 histones by cyclic AMP-dependent protein kinase reduces DNA binding. Biochim Biophys Acta. 1979 Sep 27;564(2):322–334. doi: 10.1016/0005-2787(79)90229-6. [DOI] [PubMed] [Google Scholar]
- Glotov B. O., Nikolaev L. G., Kurochkin S. N., Severin E. S. Histone Hl-DNA interaction. Influence of phosphorylation on the interaction of histone Hl with linear fragmented DNA. Nucleic Acids Res. 1977 Apr;4(4):1065–1082. doi: 10.1093/nar/4.4.1065. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goodwin G. H., Mathew C. G., Wright C. A., Venkov C. D., Johns E. W. Analysis of the high mobility group proteins associated with salt-soluble nucleosomes. Nucleic Acids Res. 1979 Dec 11;7(7):1815–1835. doi: 10.1093/nar/7.7.1815. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gurley L. R., D'Anna J. A., Barham S. S., Deaven L. L., Tobey R. A. Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells. Eur J Biochem. 1978 Mar;84(1):1–15. doi: 10.1111/j.1432-1033.1978.tb12135.x. [DOI] [PubMed] [Google Scholar]
- Holmgren P., Rasmuson B., Johansson T., Sundquist G. Histone content in relation to amount of heterochromatin and developmental stage in three species of Drosophila. Chromosoma. 1976 Feb 13;54(2):99–116. doi: 10.1007/BF00292833. [DOI] [PubMed] [Google Scholar]
- 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]
- Lamy F., Lecocq R., Dumont J. E. Thyrotropin stimulation of the phosphorylation of serine in the N-terminal of thyroid H1 histones. Eur J Biochem. 1977 Mar 1;73(2):529–535. doi: 10.1111/j.1432-1033.1977.tb11347.x. [DOI] [PubMed] [Google Scholar]
- Lawson G. M., Cole R. D. Selective displacement of histone H1 from whole HeLa nuclei: effect on chromatin structure in situ as probed by micrococcal nuclease. Biochemistry. 1979 May 29;18(11):2160–2166. doi: 10.1021/bi00578a005. [DOI] [PubMed] [Google Scholar]
- Letnansky K. Nuclear proteins in genetically active and inactive parts of chromatin. FEBS Lett. 1978 May 1;89(1):93–97. doi: 10.1016/0014-5793(78)80530-4. [DOI] [PubMed] [Google Scholar]
- Levy-Wilson B., Dixon G. H. Limited action of micrococcal nuclease on trout testis nuclei generates two mononucleosome subsets enriched in transcribed DNA sequences. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1682–1686. doi: 10.1073/pnas.76.4.1682. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Loening U. E. The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresis. Biochem J. 1967 Jan;102(1):251–257. doi: 10.1042/bj1020251. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McGhee J. D., Felsenfeld G. Nucleosome structure. Annu Rev Biochem. 1980;49:1115–1156. doi: 10.1146/annurev.bi.49.070180.005343. [DOI] [PubMed] [Google Scholar]
- Nelson D., Covault J., Chalkley R. Segregation of rapidly acetylated histones into a chromatin fraction released from intact nuclei by the action of micrococcal nuclease. Nucleic Acids Res. 1980 Apr 25;8(8):1745–1763. doi: 10.1093/nar/8.8.1745. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noll M. Internal structure of the chromatin subunit. Nucleic Acids Res. 1974 Nov;1(11):1573–1578. doi: 10.1093/nar/1.11.1573. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noll M., Kornberg R. D. Action of micrococcal nuclease on chromatin and the location of histone H1. J Mol Biol. 1977 Jan 25;109(3):393–404. doi: 10.1016/s0022-2836(77)80019-3. [DOI] [PubMed] [Google Scholar]
- Ord M. G., Stocken L. A. Nucleosomes from normal and regenerating rat liver. Biochem J. 1979 Jan 15;178(1):173–185. doi: 10.1042/bj1780173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Panyim S., Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys. 1969 Mar;130(1):337–346. doi: 10.1016/0003-9861(69)90042-3. [DOI] [PubMed] [Google Scholar]
- Rattle H. W., Langan T. A., Danby S. E., Bradbury E. M. Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Effect of A and B site phosphorylation on the conformation and interaction of histone H1. Eur J Biochem. 1977 Dec;81(3):499–505. doi: 10.1111/j.1432-1033.1977.tb11975.x. [DOI] [PubMed] [Google Scholar]
- Sanders M. M. Fractionation of nucleosomes by salt elution from micrococcal nuclease-digested nuclei. J Cell Biol. 1978 Oct;79(1):97–109. doi: 10.1083/jcb.79.1.97. [DOI] [PMC free article] [PubMed] [Google Scholar]
- See Y. P., Burrow G. N., Liew C. C. Effect of thyrotropin on the phosphorylation of thyroid chromosomal proteins. Can J Biochem. 1979 Jun;57(6):523–528. doi: 10.1139/o79-066. [DOI] [PubMed] [Google Scholar]
- Shoemaker C. B., Chalkley R. H3-specific nucleohistone kinase of bovine thymus chromatin. Purification, characterization, and specificity for threonine residue 3. J Biol Chem. 1980 Nov 25;255(22):11048–11055. [PubMed] [Google Scholar]
- Spaulding S. W., Schubart U. K. Time course of thyrotropin-dependent protein phosphorylation in thyroid slices. Endocrinology. 1978 Dec;103(6):2334–2341. doi: 10.1210/endo-103-6-2334. [DOI] [PubMed] [Google Scholar]
- Szopa J., Jacob G., Arfmann H. A. Influence of histone phosphorylation upon histone-histone interactions studied in vitro. Biochemistry. 1980 Mar 4;19(5):987–990. doi: 10.1021/bi00546a024. [DOI] [PubMed] [Google Scholar]
- 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]
- Thoma F., Koller T., Klug A. Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol. 1979 Nov;83(2 Pt 1):403–427. doi: 10.1083/jcb.83.2.403. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Whitlock J. P., Jr, Simpson R. T. Removal of histone H1 exposes a fifty base pair DNA segment between nucleosomes. Biochemistry. 1976 Jul 27;15(15):3307–3314. doi: 10.1021/bi00660a022. [DOI] [PubMed] [Google Scholar]


