Abstract
Polyclonal and monoclonal antibodies specific for histones as well as sera directed against synthetic peptides of histones were used to probe the topography of chromatin subunits. In native chromatin, the regions corresponding to residues 130-135 of H3 and 6-18 of H2B were found to be exposed and able to interact with antibodies whereas the regions 26-35 and 36-43 of H2B and 80-89 and 85-102 of H4 were not. In vitro phosphorylation of H3 and H5 in native chromatin or of H3 in H1/H5-depleted chromatin led to a marked drop in the binding of antibodies specific for residues 130-135 of H3 and 6-18 of H2B. Phosphorylation of H1/H5-depleted chromatin also altered the degree of exposure of certain H2A epitopes but it did not affect the surface accessibility of residues 1-11 of H2B.
Full text
PDF





Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Absolom D., Van Regenmortel M. H. Nucleosome structure studied with purified antibodies to histones H2B, H3 and H4. FEBS Lett. 1977 Dec 20;85(1):61–64. doi: 10.1016/0014-5793(78)81248-4. [DOI] [PubMed] [Google Scholar]
- Absolom D., van Regenmortel M. H. Purification by immunoadsorption and immunochemical properties of histone H3. FEBS Lett. 1977 Sep 15;81(2):419–422. doi: 10.1016/0014-5793(77)80568-1. [DOI] [PubMed] [Google Scholar]
- Ajiro K., Nishimoto T., Takahashi T. Histone H1 and H3 phosphorylation during premature chromosome condensation in a temperature-sensitive mutant (tsBN2) of baby hamster kidney cells. J Biol Chem. 1983 Apr 10;258(7):4534–4538. [PubMed] [Google Scholar]
- Allan J., Harborne N., Rau D. C., Gould H. Participation of core histone "tails" in the stabilization of the chromatin solenoid. J Cell Biol. 1982 May;93(2):285–297. doi: 10.1083/jcb.93.2.285. [DOI] [PMC free article] [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]
- Bakayev V. V., Bakayeva T. G., Domansky N. N. Studies on protein organization of nucleosomes using cross-linking. Mol Biol Rep. 1981 Aug 14;7(4):209–216. doi: 10.1007/BF00805754. [DOI] [PubMed] [Google Scholar]
- Boulikas T., Wiseman J. M., Garrard W. T. Points of contact between histone H1 and the histone octamer. Proc Natl Acad Sci U S A. 1980 Jan;77(1):127–131. doi: 10.1073/pnas.77.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradbury E. M., Inglis R. J., Matthews H. R., Langan T. A. Molecular basis of control of mitotic cell division in eukaryotes. Nature. 1974 Jun 7;249(457):553–556. doi: 10.1038/249553a0. [DOI] [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]
- Champagne M., Mazen A., Wilhelm X. Histones d'érythrocytes de poulets. I. Fractionnement des histones totales et isolement d'une histone spécifique. Bull Soc Chim Biol (Paris) 1968 Nov 5;50(7):1261–1272. [PubMed] [Google Scholar]
- Chatterjee S., Walker I. O. The modification of deoxyribonucleohistone by trypsin and chymotrypsin. Eur J Biochem. 1973 May 2;34(3):519–526. doi: 10.1111/j.1432-1033.1973.tb02789.x. [DOI] [PubMed] [Google Scholar]
- DeLange R. J., Williams L. C., Martinson H. G. Identification of interacting amino acids at the histone 2A--2B binding site. Biochemistry. 1979 May 15;18(10):1942–1946. doi: 10.1021/bi00577a014. [DOI] [PubMed] [Google Scholar]
- Diaz B. M., Walker I. O. Trypsin digestion of core chromatin. Biosci Rep. 1983 Mar;3(3):283–292. doi: 10.1007/BF01122461. [DOI] [PubMed] [Google Scholar]
- Finch J. T., Brown R. S., Richmond T., Rushton B., Lutter L. C., Klug A. X-ray diffraction study of a new crystal form of the nucleosome core showing higher resolution. J Mol Biol. 1981 Feb 5;145(4):757–769. doi: 10.1016/0022-2836(81)90313-2. [DOI] [PubMed] [Google Scholar]
- Goldblatt D., Bustin M. Exposure of histone antigenic determinants in chromatin. Biochemistry. 1975 Apr 22;14(8):1689–1695. doi: 10.1021/bi00679a022. [DOI] [PubMed] [Google Scholar]
- Grigoryev S. A., Krasheninnikov I. A. Transient unfolding of trypsin-digested chromatin core particles. Eur J Biochem. 1982 Dec;129(1):119–125. doi: 10.1111/j.1432-1033.1982.tb07029.x. [DOI] [PubMed] [Google Scholar]
- Hanks S. K., Rodriguez L. V., Rao P. N. Relationship between histone phosphorylation and premature chromosome condensation. Exp Cell Res. 1983 Oct 15;148(2):293–302. doi: 10.1016/0014-4827(83)90153-2. [DOI] [PubMed] [Google Scholar]
- Harborne N., Allan J. Modulation of the relative trypsin sensitivities of the core histone 'tails'. FEBS Lett. 1983 May 2;155(1):88–92. doi: 10.1016/0014-5793(83)80215-4. [DOI] [PubMed] [Google Scholar]
- Hohmann P. Phosphorylation of H1 histones. Mol Cell Biochem. 1983;57(1):81–92. doi: 10.1007/BF00223526. [DOI] [PubMed] [Google Scholar]
- Inglis R. J., Langan T. A., Matthews H. R., Hardie D. G., Bradbury E. M. Advance of mitosis by histone phosphokinase. Exp Cell Res. 1976 Feb;97(2):418–425. doi: 10.1016/0014-4827(76)90634-0. [DOI] [PubMed] [Google Scholar]
- Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krystal G. W., Poccia D. L. Phosphorylation of cleavage stage histone H1 in mitotic and prematurely condensed chromosomes. Exp Cell Res. 1981 Jul;134(1):41–48. doi: 10.1016/0014-4827(81)90461-4. [DOI] [PubMed] [Google Scholar]
- Kurochkin S. N., Andreeva N. G., Gasaryan K. G., Severin E. S., Kurchatov I. V. Investigation of sites phosphorylated in histone H5 by protein kinase from pig brain. FEBS Lett. 1977 Apr 1;76(1):112–114. doi: 10.1016/0014-5793(77)80132-4. [DOI] [PubMed] [Google Scholar]
- Lake R. S. F1-histone phosphorylation in metaphase chromosomes of cultured Chinese hamster cells. Nat New Biol. 1973 Apr 4;242(118):145–146. doi: 10.1038/newbio242145a0. [DOI] [PubMed] [Google Scholar]
- Laskov R., Muller S., Hochberg M., Giloh H., Van Regenmortel M. H., Eilat D. Monoclonal autoantibodies to histones from autoimmune NZB/NZW F1 mice. Eur J Immunol. 1984 Jan;14(1):74–81. doi: 10.1002/eji.1830140114. [DOI] [PubMed] [Google Scholar]
- Mangeat P. H., Chahinian H., Marchis-Mouren G. J. Characterization of the cyclic AMP-dependent protein kinase from rat pancreas, further purification of the catalytic subunit, substrate specificity, effect of the pancreatic heat stable inhibitor. Biochimie. 1978;60(8):777–785. doi: 10.1016/s0300-9084(78)80022-4. [DOI] [PubMed] [Google Scholar]
- Marion C., Roux B., Coulet P. R. Role of histones H1 and H3 in the maintenance of chromatin in a compact conformation. Study with an immobilized enzyme. FEBS Lett. 1983 Jul 4;157(2):317–321. doi: 10.1016/0014-5793(83)80568-7. [DOI] [PubMed] [Google Scholar]
- Marion C., Roux B., Pallotta L., Coulet P. R. Study of chromatin organization with trypsin immobilized on collagen membranes. Biochem Biophys Res Commun. 1983 Aug 12;114(3):1169–1175. doi: 10.1016/0006-291x(83)90685-x. [DOI] [PubMed] [Google Scholar]
- Martinage A., Mangeat P., Laine B., Couppez M., Sautiere P., Marchis-Mouren G., Biserte G. In vitro phosphorylation of histones H5, H2A, H2B and of the dimer H2A--H2B by a cyclic AMP-dependent protein kinase from rat pancreas. FEBS Lett. 1980 Sep 8;118(2):323–329. doi: 10.1016/0014-5793(80)80249-3. [DOI] [PubMed] [Google Scholar]
- Martinage A., Mangeat P., Sautiere P., Couppez M., Marchis-Mouren G., Biserte G. Study of in vitro phosphorylation of histones H3, H4 and of the non-acetylated and acetylated tetramers (H3-H4)2. FEBS Lett. 1981 Nov 2;134(1):107–110. doi: 10.1016/0014-5793(81)80562-5. [DOI] [PubMed] [Google Scholar]
- Matsumoto Y., Yasuda H., Mita S., Marunouchi T., Yamada M. Evidence for the involvement of H1 histone phosphorylation in chromosome condensation. Nature. 1980 Mar 13;284(5752):181–183. doi: 10.1038/284181a0. [DOI] [PubMed] [Google Scholar]
- Mazen A., Champagne M. Histones d'érythrocytes de poulets. IV. Etude quantitative des histones au cours de la maturation des érythrocytes. Biochimie. 1972;54(10):1273–1279. doi: 10.1016/s0300-9084(72)80068-3. [DOI] [PubMed] [Google Scholar]
- Mazen A., De Murcia G., Bernard S., Pouyet J., Champagne M. Localization of histone H5 in the subunit organization of chromatin using immunoelectron microscopy. Eur J Biochem. 1982 Sep;127(1):169–176. doi: 10.1111/j.1432-1033.1982.tb06852.x. [DOI] [PubMed] [Google Scholar]
- Muller S., Erard M., Burggraf E., Couppez M., Sautière P., Champagne M., Van Regenmortel M. H. Immunochemical detection of changes in chromatin subunits induced by histone H4 acetylation. EMBO J. 1982;1(8):939–944. doi: 10.1002/j.1460-2075.1982.tb01275.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Muller S., Himmelspach K., Van Regenmortel M. H. Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits. EMBO J. 1982;1(4):421–425. doi: 10.1002/j.1460-2075.1982.tb01185.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Muller S., Soussanieh A., Bouley J. P., Reinbolt J., Van Regenmortel M. H. Localization of two antigenic determinants in histone H4. Biochim Biophys Acta. 1983 Sep 14;747(1-2):100–106. doi: 10.1016/0167-4838(83)90127-9. [DOI] [PubMed] [Google Scholar]
- Nelson N. C., Taylor S. S. Differential labeling and identification of the cysteine-containing tryptic peptides of catalytic subunit from porcine heart cAMP-dependent protein kinase. J Biol Chem. 1981 Apr 25;256(8):3743–3750. [PubMed] [Google Scholar]
- Paulson J. R., Taylor S. S. Phosphorylation of histones 1 and 3 and nonhistone high mobility group 14 by an endogenous kinase in HeLa metaphase chromosomes. J Biol Chem. 1982 Jun 10;257(11):6064–6072. [PubMed] [Google Scholar]
- Pospelov V. A., Svetlikova S. B., Vorob'ev V. I. Nucleosome-nucleosome interaction in chromatin. FEBS Lett. 1979 Mar 1;99(1):123–128. doi: 10.1016/0014-5793(79)80263-x. [DOI] [PubMed] [Google Scholar]
- Rill R. L., Oosterhof D. K. The accessibilities of histones in nucleosome cores to an arginine-specific protease. J Biol Chem. 1982 Dec 25;257(24):14875–14880. [PubMed] [Google Scholar]
- Ring D., Cole R. D. Chemical cross-linking of H1 histone to the nucleosomal histones. J Biol Chem. 1979 Nov 25;254(22):11688–11695. [PubMed] [Google Scholar]
- Romac J., Bouley J. P., Van Regenmortel M. H. Enzyme-linked immunosorbent assay in the study of histone antigens and nucleosome structure. Anal Biochem. 1981 May 15;113(2):366–371. doi: 10.1016/0003-2697(81)90090-7. [DOI] [PubMed] [Google Scholar]
- Russo E., Giancotti V., Crane-Robinson C., Geraci G. Histone H1 and chromatin higher order structure. Does histone H1 exhibit specific self-association? Int J Biochem. 1983;15(4):487–493. doi: 10.1016/0020-711x(83)90121-0. [DOI] [PubMed] [Google Scholar]
- Saccone G. T., Skinner J. D., Burgoyne L. A. Resistance of chromatin superstructure to tryptic digestion modulated by conjugated polyacrylamide. FEBS Lett. 1983 Jun 27;157(1):111–114. doi: 10.1016/0014-5793(83)81126-0. [DOI] [PubMed] [Google Scholar]
- Stollar B. D., Ward M. Rabbit antibodies to histone fractions as specific reagents for preparative and comparative studies. J Biol Chem. 1970 Mar 25;245(6):1261–1266. [PubMed] [Google Scholar]
- Strätling W. H. Role of histone H1 in the conformation of oligonucleosomes as a function of ionic strength. Biochemistry. 1979 Feb 20;18(4):596–603. doi: 10.1021/bi00571a008. [DOI] [PubMed] [Google Scholar]
- Suda M., Iwai K. Identification of suberimidate cross-linking sites of four histone sequences in H1-depleted chromatin. Histone arrangement in nucleosome core. J Biochem. 1979 Dec;86(6):1659–1670. doi: 10.1093/oxfordjournals.jbchem.a132686. [DOI] [PubMed] [Google Scholar]
- Sung M. T., Freedlender E. F. Sites of in vivo phosphorylation of histone H5. Biochemistry. 1978 May 16;17(10):1884–1890. doi: 10.1021/bi00603a013. [DOI] [PubMed] [Google Scholar]
- Taylor S. S. The in vitro phosphorylation of chromatin by the catalytic subunit of cAMP-dependent protein kinase. J Biol Chem. 1982 Jun 10;257(11):6056–6063. [PubMed] [Google Scholar]
- Thoma F., Koller T. Influence of histone H1 on chromatin structure. Cell. 1977 Sep;12(1):101–107. doi: 10.1016/0092-8674(77)90188-x. [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]
- Thoma F., Koller T. Unravelled nucleosomes, nucleosome beads and higher order structures of chromatin: influence of non-histone components and histone H1. J Mol Biol. 1981 Jul 15;149(4):709–733. doi: 10.1016/0022-2836(81)90354-5. [DOI] [PubMed] [Google Scholar]
- Thoma F., Losa R., Koller T. Involvement of the domains of histones H1 and H5 in the structural organization of soluble chromatin. J Mol Biol. 1983 Jul 5;167(3):619–640. doi: 10.1016/s0022-2836(83)80102-8. [DOI] [PubMed] [Google Scholar]
- Thornton J. M., Sibanda B. L. Amino and carboxy-terminal regions in globular proteins. J Mol Biol. 1983 Jun 25;167(2):443–460. doi: 10.1016/s0022-2836(83)80344-1. [DOI] [PubMed] [Google Scholar]
- Worcel A., Benyajati C. Higher order coiling of DNA in chromatin. Cell. 1977 Sep;12(1):83–100. doi: 10.1016/0092-8674(77)90187-8. [DOI] [PubMed] [Google Scholar]
- Wright E. B., Olins D. E. Histone stoichiometry in chicken erythrocyte nuclei. Biochem Biophys Res Commun. 1975 Apr 7;63(3):642–650. doi: 10.1016/s0006-291x(75)80432-3. [DOI] [PubMed] [Google Scholar]
- Zalenskaya I. A., Pospelov V. A., Zalensky A. O., Vorob'ev V. I. Nucleosomal structure of sea urchin and starfish sperm chromatin. Histone H2B is possibly involved in determining the length of linker DNA. Nucleic Acids Res. 1981 Feb 11;9(3):473–487. doi: 10.1093/nar/9.3.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
- di Padua Mathieu D., Mura C. V., Frado L. L., Woodcock C. L., Stollar B. D. Differing accessibility in chromatin of the antigenic sites of regions 1-58 and 63-125 of histone H2B. J Cell Biol. 1981 Oct;91(1):135–141. doi: 10.1083/jcb.91.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
