Abstract
Albrecht Kossel discovered a new class of basic proteins known as histones among the nuclear proteins of goose erythrocytes in 1884 (155). In 1900 Traube reported the chemical synthesis and definitive identification of a white crystalline alkaloid called theophylline, which is one of the active ingredients of tea. According to Hnilica (122) theophylline was also discovered in Kossel’s laboratoy. We shall see by the end of this paper that it is possible to use theophylline in cells to determine one of the important functions of the histones and that it is quite intriguing that both of these apparently unrelated discoveries came from the same source.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adesnik, M., Darnell, J.E.: The biogenesis and characterization of histone mRNA in Hela cells. J. Molec. Biol. 67, 397–406 (1972).
Adesnik, M., Salditt, M., Thomas, W., Darnell, J.E.: Evidence that all messenger RNA molecules (except histone messenger RNA) contain poly (A) sequences and that poly (A) has a nuclear function. J. Molec. Biol. 71, 21–30 (1972).
Adler, A.J., Langan, T.A., Fasman, G.D.: Complexes of DNA with lysine-rich (F1) histone phosphorylated at two seperate sites: circular dichroism studies. Arch. Biochem. Biophys. 153, 769–777 (1972).
Alexander, P., Horning, E. S.: Observations on the Oppenheimer method of inducing tumors by subcutaneous implantation of plastic films. In: Carcinogenesis: Mechanisms of Action (Wolstenholm and O’Conner, Eds.), CIBA Foundation Symposium, pp. 12–22. London: Churchill 1959.
Alfagene, C.R., Zweidler, , A., Mahowald, A., Cohen, L.H.: Histones of Drosophila Embryos: Electrophoretic Isolation and Structural Studies. J. Biol. Chem. Submitted (1974).
Alfret, M.: Quantitative cytochemical studies on patterns of nuclear growth. In: Fine Structure of Cells, pp. 137–163. New York: Interscience 1955.
Allfrey, V.G., Littau, V.C., Mirsky, A.E.: On the role of histonesin regulating ribonucleic acid synthesis in the cell nucleus. Proc. Natl. Acad. Sci. U.S. 49, 414–421 (1963).
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. 51, 786–794(1964).
Ajiro, K., Zweidler, A., Borun, T. W.: The identification of the messenger RNA species for individual human histone polypeptide classes. In preparation (1974).
Anderson, W.B., Rüssel, T.R., Carchman, R. A., Pastan, I.: Interrelationship between Adenylate Cyclase Activity, Adenosine 3′:5′ cyclic Monophosphate Phosphodiesterase Activity, Adenosine 3′: 5′ cyclic monophosphate levels and growth of Cells in Culture. Proc. Natl. Acad. Sci. U.S. 70, 3802–3805.
Antopova, E.N., Bogdanov, Yu.F.: Cytophotometry of DNA and Histone in meiosis of Pyrrhocoris apterus. Exp. Cell Res. 60, 40–44 (1970).
Appels, R., Well, J.R.E.: Synthesis and turnover of DNA bound-histone during maturation of Avian red blood cells. J. Mol. Biol. 20, 425–434 (1972).
Asao, T.: Regional histone changes in embryos of the newt Triturus pyrrhogaster during early development. Exp. Cell Res. 61, 255–265 (1970).
Axel, R., Cedar, H., Felsenfeld, G.: Synthesis of globin RNA from duck reticulocyte chromatin in vitro. Proc. Natl. Acad. Sci. U.S. 70, 2029–2032 (1973).
Balhorn, R., Rieke, W.O., Chalkley, R.: Rapid electrophoretic analysis for histone phosphorylation. A reinvestigation of phosphorylation of lysine-rich histone during at liver regeneration. Biochem. 10, 3952–3959 (1971).
Balhorn, R., Chalkley, R., Granner, D.: Lysine-rich histone: A positive correlation with cell replication. Biochemistry 11, 1095–1098 (1972).
Balhorn, R., Bordwell, J., Sellers, L., Granner, D., Chalkley, R.: Histone phosphorylation and DNA synthesis are linked in synchronous cultures of HTC cells. Biochem. Biophys. Res. Commun. 46, 1326–1333 (1972).
Balhorn, R., Balhorn, M., Morris, H.P., Chalkley, R.: High resolution electrophoresis of tumor histones: Variation in phosphorylation as a function of cell replication rate. Cancer Res. 32, 1775–1784 (1972).
Balhorn, R., Tanphaichitr, N., Chalkley, R., Granner, D.: The effect of inhibition of deoxyribonucleic acid synthesis on histone phosphorylation. Biochemistry 12, 5146–5150 (1973).
Baserga, R., Costlow, M., Rovera, G.: Changes in membrane function and chromatin template activity in diploid and transformed cells in culture. Federation Proc. a32, 2115–2118 (1973).
Bases, R., Mendez, F.: Dissociation of histone and DNA synthesis in irradiated Heia S-3 cells. Exptl. Cell Res. 69, 289–294 (1971).
Beisson, J., Sonneborn, T.M.: Cytoplasmic inheritance of the organization of the cell cortex in Paramecium aurelia. Proc. Natl. Acad. Sci. U.S. 53, 275–282 (1965).
Billet, M. A., Hindley, J.: A study of the quantitative variation of the histones and their relationship to RNA synthesis during erythropoisis in the adult chicken. European J. Biochem. 28, 451–462 (1972).
Bloch, D.P., Godman, G.C.: A microspectrophotometric study of the synthesis of des-oxyribonucleic acid and nuclear histone. J. Biophys. Biochem. Cytol. 1, 17–28 (1955).
Bloch, D.P., Brack, S.D.: Evidence for the cytoplasmic synthesis of nuclear histone during spermigonesis in the grasshopper Chortophaga vividifasciata (de Geer). J. Cell Biol. 22, 327–340 (1964).
Bloch, D.P., Macquigg, R.A., Brack, S.D., Wu, J.-R.: The synthesis of Deoxyribonucleic acid and histone in the onion root meristem. J. Cell Biol. 33, 451–466 (1967).
Bloch, D.P., Teng, C.: The synthesis of deoxyribonucleic acid and nuclear histone of the X-chromosome of the Rhenia spinosus spermatocyte. J. Cell Science 5, 321–332 (1969).
Boganov, Yu.F., Liapunova, N.A., Sherudilo, Antropova, E. N.: Uncoupling of DNA and histone synthesis prior to Prophase I of Meiosis in the cricket Grillus(Ache-ta)Domestica L. Exp. Cell Res. 52, 59–70 (1968).
Bonner, J., Chalkley, G.R., Dahmus, M., Fambrough, D., Kujimura, F., Huang, R.C.C., Huberman, J., Jensen, R., Marushige, K., Colenbush, H., Olivera, B.M., Widholm, J.: Isolation and characterization of chromosomal nucleoproteins. In: Grossman, L., Moldave, K. (Eds.): Methods in Enzymology, Vol. 12b, p.3ff. New York: Academic Press 1968.
Borun, T.W., Scharff, M.D., Robbins, E.: Rapidly-labeled, polyribosome-associated RNA having the properties of histone messenger. Proc. Natl. Acad. Sci. U.S. 58, 1977–1983(1967).
Borun, T.W., Baserga, R.: Unpublished observations.
Borun, T.W., Stein, G. S.: The synthesis of acidic chromosomal proteins during the cell cycle of Hela S-3 cells. II. The kinetics of residual protein synthesis and transport. J. Cell Biol. 52, 308–315 (1972).
Borun, T.W., Pearson, D.B., Paik, W.K.: Studies of histone methylation during the Hela S-3 cell cycle. J. Biol. Chem. 247, 4288–4298 (1972).
Borun, T.W., Paik, W.L., Lee, H.W., Pearson, D.B., Marks, D.: Histone methylation and Phosphorylation during the Hela S-3 cell cycle. In: The Control of Proliferation in Animal Cells. First Cold Spring Harbor Symposium 1973.
Borun, T.W., Marks, D.: Histone F1 phosphorylation is a necessary but not sufficient cause of DNA replication in the Hela S-3 cell. (In preparation) (1974).
Borun, T.W., Paik, W.K., Marks, D.: Histone phorylation and the control of cellular proliferation. In: Mehlman, M.A., Hansen, R.W. (Eds.): Control Processes in Neoplasia. New York: Academic Press 1974.
Borun, T.W., Pan, C.J., Ajiro, K.: The isolation of human histone messenger RNA. (In preparation) (1974).
Borun, T.W., Gabrielli Ajiro, K., Zweidler, A., Baglioni, C.: Studies on the transla-tional control of histone synthesis. III. Translation of histone messenger RNA isolated from polyribosomes and postribosomal supernatante of synchronized Hela S-3 cells. (In preparation) (1974).
Borun, T.W.: Unpublished observations.
Bradbury, E.M., Molgaard, H.V., Stephens, R.M., Boland, L.A., Johns, E.W.: X-ray studies of nucleoproteins depleted of lysine-rich histone. European J. Biochem. 31 474–482(1972).
Bradbury, E.M., Inglis, R.J., Matthews, H.R., Sarner,N.: Phosphorylation of very-lysine-rich histone in Physarum polycephalum. European J. Biochem. 33,
Breindl, M., Gallwitz, D.: Identification of histone messenger RNA from Hela cells. Appearance of histone m-RNA in the cytoplasm and its translation in a rabbit reticulocyte, cell-free system. European J. Biochem. 32, 381–391 (1973).
Bril-Peterson, R., Westerbrink, H.G.K.: A structural basic protein as a counterpart of deoxyribonucleic acid in mammalian spermatazoa. Biochim. Biophys. Acta 76, 152–154(1963).
Burnett, G.K., Kennedy, E.P.: The enzymatic phosphorylation of proteins. J. Biol. Chem. 211, 969–980 (1954).
Busch, H.: Histones and other Nuclear Proteins. New York: Academic Press 1965.
Bustin, M, Cole, R.D.: Bisection of a lysine-rich histone by N-bromosuccinimide. J. Biol. Chem. 244, 5291–5299 (1969).
Bustos-Valdes, S.E., Deisseroth, A., Dounce, A.L.: Metabolic studies of histones and residual proteins of rat liver nuclei. Arch. Biochem. Biophys. 126, 848–855 (1968).
Butler, J.A.V, Davidson, P.F, James, D.W.F., Shooter, K.V.: The histones of calf thymus deoxyribonucleoprotein. I. Preparation and homogeneity. Biochim. Biophys. Acta 13, 224–232 (1954).
Butler, J.A.V., Cohn, P., Simson, P.: The presence of basic proteins in microsomes. Biochim. Biophys. Acta 38, 386–388 (1960).
Butler, J.A.V., Cohn, P.: Studies on histones. 6. Observations on the biosynthesis of histones and other proteins in regenerating rat liver. Biochem. J. 87, 330–334 (1963).
Butler, W.B., Mueller, G.C.: Control of histone synthesis in Hela cells. Biochim. Biophys. Acta 294, 481–496 (1973).
Byrd, Jr., E.W., Kasinsky, H.E.: Histone synthesis during early embryogenesis Xeno-pus laevis (South African clawed toad). Biochemistry 12, 246–253 (1973).
Byvoet, P.: Metabolic integrity of deoxyribonucleohistones. J. Molec. Biol. 17, 311–318(1966).
Byvoet (Bijvoet), P.: Metabolic integrity of deoxyribonucleohistones during enzyme induction. Molec. Pharmacol. 3, 303–305 (1967).
Chae, C.B., Williams, A., Krasny, H., Irvin, J.L., Piantadosi, C.: Inhibition of thymidine phsophorylation and DNA and histone synthesis in Ehrlich ascites tumor cells. Cancer Res. 30, 2652–2660 (1970).
Chae, C.B., Smith, M.C., Irvin, J.L.: Effect of in vitro histone phosphorylation on template activity of rat liver chromatin. Biochim. Biophys. Acta 287, 134–153 (1972).
Chalkley, G.R., Maurer, H.R.: Turnover of template-bound histone. Proc. Natl. Acad. Sci. (U.S. 54, 498–505 (1965).
Champagne, M., Pouyet, J., Ouellet, L., Garel, A.: Histones d’erythrocytes de poulets. II. Etude physiochemique de l’histone specific. Bull. Soc. Chem. Biol. 52, 377(1970).
Cognetti, G., Settineri, D., Spinelli, G.: Developmental changes of chromatin nonhistone proteins in sea urchins. Exp. Cell Res. 71, 465–467 (1972).
Cohen, L.H., Gotchel, B.V.: Histones of polytene and non-polytene nuclei of Droso-phila melanogaster. J. Biol. Chem. 246, 1841–1848 (1971).
Cook, P.R.: Hypothesis on differentiation and the inheritance of gene superstructure. Nature 245,23–25 (1973).
Cozeolluella, C., Subirana, J. A.: Somatic histones from Mytilus edulis. Biochim. Biophys. Acta 154, 242–244 (1968).
Craig, N., Kelly, D.E., Perry, R.P.: Lifetime of messenger RNAs which code for ribo-somal proteins in the L’cell. Biochim. Biophys. Acta 246, 493–498 (1971).
Crampton, C.F., Moore, S., Stein, W.H.: Chromatographic fractionation of calf thymus histone. J. Biol. Chem. 215, 787–801 (1955).
Crampton, C.F., Stein, W.H., Moore, S.: Comparative studies on chromatograph-ically purified histones. J. Biol. Chem. 225, 363–385 (1957).
Cross, M.E.: Changes in nuclear protein during the cell cycle in cultured mast cells separater by zonal centrifugation. Biochem. J. 128, 1213–1219 (1972).
Das, N.K., Alfert, M.: Cytochemical studies on the concurrent synthesis of DNA and histone in primary spermatocytes of Urechis caupo. Exp. Cell Res. 49, 51–59 (1968).
Davidson, P. F.: Histones from normal and malignant cells. Biochem. J. 66, 703–707 (1957).
Davidson, P.F.: Chromatography of histones. Biochem. J. 66, 708–712 (1957).
Davis, B.: Disc electrophoresis. II. Methods and application to human serum proteins. Ann. N.Y. Acad. Sci. 121, 404–427 (1964).
Delange, R.J., Fambrough, D.M., Smith, E., Bonner, J.: Calf and pea histone IV (f2al). I. Amino acid compositions of the identical COOH terminal 19 residue sequence. J. Biol. Chem. 243, 5906–5913 (1968).
Delange, R.J., Smith, E.L., Fambrough, D.M., Bonner, J.: Amino acid sequence of histone IV (f2al): Presence of-N-acetyllysine. Proc. Natl. Acad. Sci. U.S. 61, 1145–1152 (1968).
Delange, R.J., Fambrough, D.M., Smith, E.L., Bonner, J.: Calf and pea thymus histone IV (f2al). The complete amino acid sequence of call thymus histone IV (f2al). Presence of-N-acetyllysine. J. Biol. Chem. 244, 319–334 (1969).
Delange, R.J., Smith, E.L., Bonner, J.: Calf thymus histone. III. Sequence of the amino and carboxyl terminal regions containing lysyl residues modified by acetylation and methylation. Biochem. Biophys. Res. Comm. 40, 989–993 (1970)
See also Hooper, J. A., Smith, E.L., Sommer, K.R., and Chalkley, R.: Amino acid sequence of histone III of the testis of the carp, Leuobus bubalus. J. Biol. Chem. 248, 3275–3279 (1973).
Dick, C., Johns, E.W.: The biosynthesis of the five main histone fractions of rat thymus. Biochim. Biophys. Acta 174, 380–386 (1969).
Diggle, J.H., Peacock, A.R.: The molecular weights and association of histones of chicken erythrocytes. FEBS Letters 18, 138 (1971).
Elgin, S.C.R., Hood, L.E.: Chromosomal proteins of Drosophila embryos. Biochemistry 12, 4984–4991 (1973).
Fambrough, D.M., Bonner, J.: On the similarity of plant and animal histones. Biochemistry 5, 2563–2570 (1966).
Fambrough, D.M., Fujimura, F., Bonner, J.: Quantitative distribution of histone components in plants. Biochemistry 7, 575–585 (1968).
Fambrough, D.M., Bonner, J.: Sequence homology and the role of cysteine in plant and animal arginine-rich histone (f3). J. Biol. Chem. 243, 4434–4439 (1968).
Faquhar, M.N., McCarthy, B.J.: Histone mRNA in eggs and embryos of Stronglo centrotus purpuratus. Biochem. Biophys. Res. Commun. 53, 515–522 (1973).
Flamm, W.G., Birnstiel, M.L.: Inhibition of DNA replication and its effect on histone synthesis. Exptl. Cell Res. 33, 658–660 (1964).
Gall, J.: Macronuclear duplication in the ciliated protozoan Euplotes. J. Biophys. Biochem. Cytol. 5, 295–308 (1959).
Gallwitz, D., Mueller, G.C.: Histone synthesis in vitro by cytoplasmic microsomes from Hela cells. Science 163, 1351–1353 (1969).
Gallwitz, D., Mueller, G.C.: Histone synthesis in vitro on Hela cell microsomes. The nature of the coupling to deoxyribonucleic acid synthesis. J. Biol. Chem. 244, 5947–5952 (1969).
Gallwitz, D., Mueller, G.C.: RNA from Hela cell microsomes with properties of histone messenger. FEBS Letters 6, 83–85 (1970).
Gallwitz, D., Breindl, M.: Synthesis of histones in a rabbit reticulocyte cell-free system directed by a polyribosomal RNA fraction from synchronized Hela cells. Biochem. Biophys. Res. Commun. 47, 1106–1111 (1972).
Gautschi, J.R., Kern, R.M.: DNA replication in mammalian cells in the presence of cycloheximide. Exp. Cell Res. 80, 15–26 (1973).
Gavosto, T., Pegoraro, L., Masera, P., Rovera, G.: Late DNA replication pattern in human haemopoietic cells. A comparitive investigation using high resolution quantitative autoradiography. Exp. Cell 49, 340–358 (1968).
Gerner, E.W., Humphrey, R.M.: The cell cycle phase synthesis of non-histone proteins in mammalian cells. Biochim. Biophys. Acta 331, 117–127 (1973).
Gershey, E.L., Vidali, G., Allfrey, V.G.: Chemical studies of histone acetylation. The occurance of -N-acetyllysine in the f histone. J. Biol. Chem. 243, 5018–5027 (1968).
Gershey, E.L., Haslett, G.W., Vidali, G., Allfrey, V.C.: Chemical studies of histone methylation. Evidence for occurance of 3-methylhistidine in avian erythrocytes histones. J. Biol. Chem. 244, 4871–4877 (1969).
Gilmour, R.S., Paul, J.: RNA transcribed from reconstructed nucleoprotein is similar to natural RNA. J. Molec. Biol. 40, 137–142 (1969).
Gilmour, R.S., Paul, J.: Tissue specific transcription of the globin gene in isolated chromatin. Proc. Natl. Acad. Sci. U.S. 70, 3440–3442 (1973).
Greenberg, J.R., Perry, R.P.: Relative occurance polyadenylic acid sequences in messenger RNA and heterogeneous nuclear RNA of L cells as determined by poly(U) hydroxylapatite chromatography. J. Molec. Biol. 72, 91–98 (1972).
Greenway, P.J., Murray, K.: Polynucleotides associated with histone preparations. Biochem. J. 131, 585–591 (1973).
Griffin, A.C., Ward, V.C., Wade, J., Ward, D.N.: Synthesis and release of basic proteins or peptides by tumor ribosomes. Biochim. Biophys. Acta 72, 500–503 (1963).
Gross, K.W., Rudderman, J., Jacobs-Lorena, M., Baglioni, C., Gross, P.R.: Cellfree synthesis of histones by messenger RNA from sea urchin embryos. Nature 241, 272–274 (1973).
Gross, K.W., Jacobs-Lorena, M., Baglioni, C., Gross, P.R.: Cell-free translation of maternal messenger RNA from sea urchin. Proc. Natl. Acad. Sci. U.S. 70, 2614–2618 (1973).
Grunstein, M., Levy, S., Schedl, P., Kedes, L.: Messenger RNA for individual histone proteins: fingerprint analysis and in vitro translation. In: The organization of genetic material in eucaryotex. 38th Cold Spring Harbor Symposium on Quantitative Biology.
Gurley, L.R., Hardin, J.M.: The metabolism of histone fractions. I. Synthesis of histone fractions during the life cycle of mammalian cells. Arch. Biochem. Biophys.
Gurley, L.R., Hardin, J.M.: The metabolism of histone fractions. II. Conservation and turnover of histone fractions in mammalian cells. Arch. Biochem. Biophys.
Gurley, L.R., Hardin, J.M.: The metabolism of histone fractions. III. Synthesis and turnover of histone F1. Arch. Biochem. Biophys. 136, 392–401.
Gurley, L.R., Walters, R.A., Enger, M.D.: Isolation and characterization of f1 on ribosomes. Biochem. Biophys. Res. Commun. 40, 428–436 (1970).
Gurley, L.R., Walters, R.A.: Response of histone turnover and phosphorylation to X-irradiation. Biochemistry 10, 1588–1593 (19).
Gurley, L.R., Walters, R.A., Tobey, R.A.: The metabolism of histone fractions. IV. Synthesis of histones during the G1 phase of the mammalian life cycle. Arch. Biochem. Biophys. 148, 633–641 (1972).
Gurley, L.R., Walters, R.A.: The metabolism of histone fractions. V. Relationship between histone and DNA synthesis after X-irradiation. Arch. Biochem. Biophys. 153, 304–311(1972).
Gurley, L.R., Walters, R. A., Tobey, R.A.: Histone phosphorylation in late interphase and mitosis. Biochem. Biophys. Res. Commun. 50, 744–750 (1973).
Gurley, L.R., Walters, R.A., Tobey, R.A.: The metabolism of histone fractions. VI. Differences in the phosphorylation of histone fractions during the cell cycle. Arch. Biochem. Biophys. 154, 212–218 (1973).
Gurley, L.R., Enger, M.D., Walters, R.A.: The nature of histone F1 isolated from polysomes. Biochemistry 12, 237–245 (1973).
Gurley, L.R., Walters, R. A., Tobey, R.A.: Cell cycle-specific changes in histone phosphorylation associated with cell proliferation and chromosomes condensation. J. Cell Biol. (In press) (1974).
Hancock, R.: Conservation of histones in chromatin during growth and mitosis in vitro. J. Molec. Biol. 40, 457–466 (1969).
Hardin, J.A., Einem, G.E., Lindsay, D.T.: Simultaneous synthesis of histone and DNA in synchronously dividing Tetrahymena pyriformis. J. Cell Biol. 33 709–717 (1967).
Harris, M.: The initiation of deoxyribonucleic acid synthesis in the connective tissue cell with some observations on the function of the nucleolus. Biochemistry J. 72, 54–60 (1959).
Hempel, K., Lange, H.W., Birkofer, L.: ε-N-Trimethyllysin, eine neue Aminosäure in Histonen. Naturwissenschaften 55, 37 (1968).
Henricks, D.M., Mayer, D.T.: Isolation and characterization of a basic keritinlike protein from mammalian spermatozoa. Exptl. Cell Res. 40, 402–410 (1965).
Hereford, L.M., Hartwell, L.H.: Role of protein synthesis in the replication of yeast DNA. Nature 244, 129–131 (1973).
Highfield, D.R, Dewey, W.C.: Inhibition of DNA synthesis in synchronized Chinese hamster cells treated in G1 or early S phase with cycloheximide or puromycin. Exptl. Cell Res. 75, 314–320 (1972).
Hnilica, L.S., Johns, E.W., Butler, J.A.V.: Observations on the species and tissue specificity of histones. Biochem. J. 82, 123–129 (1962).
Hnilica, L.S.: The specificity of histones in chicken erythrocytes. Experientia 20, 13–14 (1964).
Hnilica, L.S., Bess, C.G.: The heterogeniety of arginine-rich histone. Analyt. Biochem. 12, 421–436 (1965).
Hnilica, L.S.: The structure and biological function of the histones. Cleveland: C.R.C. Press 1972.
Holbrook, D.J., Evans, J.H., Irvin, J.L.: Incorporation of labeled precursors into proteins and nucleic acids in regenerating rat liver. Exptl. Cell Res. 28, 120 (1962).
Holtzer, H.: Comments on induction during cell differentiation. In: Induktion und Morphogenese. 13th Colloquinum der Gesellschaft für Physiologische Chemie. Berlin-Göttingen-Heidelberg: Springer 1962.
Holtzer, H., Mayne, R., Weintraub, H., Campbell, G.: Obligatory requirement for DNA synthesis during myogenesis, erythrogenesis and chondrogenesis. In: Biochemistry of Gene Expression in Higher Organisms (Pollack A and Lee A, Eds.). Australia and New Zealand Book Co. 287–304 (1973).
Hodge, L.D., Borun, T.W., Robbins, E., Scharff, M.D.: Studies on the regulation of DNA and proteins in synchronized Hela cells. In: Biochemistry of the Cell Cycle (Ba-serga,R., Ed.), Chap. II, p. 15ff. Springfield, Ill.: Thomas 1969.
Hori, T-A., Lark, K.G.: Effect of puromycin on DNA replication in Chinese hamster cells. J. Molec. Biol. 77, 391–404 (1973).
Howard, A., Pelc, S.R.: Synthesis of desoxyribonucleic acid in normal and irradiated cells and its relationship to chromosome breakage. Heredity London (Suppl.) 6, 261–273 (1953).
Huang, R.C.C., Bonner, J.: Histone, a suppressor of chromosomal RNA synthesis. Proc. Natl. Acad. Sci. U.S. 48, 1216–1222 (1962).
Huberman, J.A., Riggs, A.D.: On the mechanism of DNA replication in mammalian chromosomes. J. Molec. Biol. 32, 327–341 (1968).
Hust, R.K., Jacobson, M.: Specification of positional information in retinal ganglion cells of Xenopus: assays for analysis of the unspecified state. Proc. Natl. Acad. Sci. U.S. 70, 507–511 (1973).
Hyodo, M., Flickinger, R.A.: Replicon growth rates during DNA replication in developing frog embryos. Biochim. Biophys. Acta 299, 29–33 (1973).
Ishikawa, H., Bishoff, R., Holtzer, H.: Mitosis and intermediate sized filiments in developing skeletal muscle. J. Cell Biol. 38, 538–555 (1968).
Iwai, K., Ishikawa, K., Hayashi, H.: Amino acid sequence of slightly lysine rich histone (f2b). Nature 226, 1056–1058 (1970).
Jacob, F., Manod, J.: Genetic regulatory mechanisms in the synthesis of proteins. J. Molec. Biol. 3, 318–356 (1961).
Jacobs-Lorena, M., Baglioni, C., Borun, T.W.: The translation of messenger for histories from Hela cells by a cell-free extract from ouse ascites tumor. Proc. Natl. Acad. Sci. U.S. 69, 2095–2099 (1972).
Jacobs-Lorena, M., Gabrielli, F., Borun, T.W., Baglioni, C.: Studies on the translation of histone messenger RNA by heterologous cell-free systems prepared from cells inactive in DNA synthesis. Biochim. Biophys. Acta 324, 275–281 (1973).
Johns, E.W., Phillips, D.M.P., Simson, P., Butler, J.A.V.: Improved fractionation of arginine rich histones from calf thymus. Biochem. J. 77, 631–636 (1960).
Johns, E.W., Butler, J.A.V.: Further fractionation of histones from calf thymus. Biochem. J. 82, 15–18 (1962).
Johns, E.W.: Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem. J. 92, 55–59 (1964).
Johns, E.W.: Studies on histones. 8. A degradation product of lysine-rich histone. Biochem. J. 93, 161–163 (1964).
Johns, E.W.: The electrophoresis of histones in Polyacrylamide gels and their quantitation. Biochem. J. 104, 78–82 (1967).
Johns, E.W., Forrester, S.: Studies of nucleoproteins. The binding of extra acidic proteins to DNA during preparation of nuclear proteins. European J. Biochem. 8, 547–551 (1969).
Jones, R.B., Irvin, J.L.: Effect of hydrocortisone on the synthesis of DNA and histones and the acetylation of histones in regenerating liver. Arch. Biochem. Biophys. 152, 828–838(1972).
Keevert, J.B., Gorovsky, M.A.: Studies on histone f1 in Tetrahymena nuclei. 13th Annual Meeting, American Society for Cell Biology, Abstract 233 (1973).
Kedes, L.H., Gross, P.R.: Identification in cleavage embryos of the three RNA species serving as templates for the synthesis of nuclear proteins. Nature 223, 1335–1339 (1969).
Kedes, L.H., Gross, P.R., Cognetti, G., Hunter, A.L.: Synthesis of nuclear ad chromosomal proteins on light polyribosomes during cleavage in the sea urchin embryo. J. Molec. Biol. 45, 337–351 (1969).
Kedes, L.H., Birnstiel, M.L.: Reiteration and clustering of DNA sequences complementary to histone messenger RNA. Nature 230, 165–169 (1971).
Kemper, B., Rich, A.: Identification of presumptive histone messenger RNA in rapidly labeled polysomal RNA of mouse myelomas. Biochim. Biophys. Acta 319, 364–372 (1973).
Kinkade, J.M., Cole, R.D.: The resolution of four lysine-rich histones derived from calf thymus. J. Biol. Chem. 241, 5790–5797 (1966).
Kinkade, J.M., Cole, R.D.: A structural comparison of different lysine-rich histones of calf thymus. J. Biol. Chem. 241, 5798–5805 (1966).
Kinkade, J.M.: Qualitative species differences and quantitative tissue differences in the distribution of lysine-rich histones. J. Biol. Chem. 244, 3375–3386 (1969).
Kinkade, J.M.: Differences in the quantitative distribution of lysine-rich histones in neoplastic and normal tissues. Proc. Soc. Exptl. Biol. Med. 137, 1131–1134 (1971).
Kleinsmith, L.J., Allfrey, V.G., Mirsky, A.E.: Phosphoprotein metabolism in isolated lymphocyte nuclei. Proc. Natl. Acad. Sci. U.S. 55, 1182–1189 (1966).
Kossel, A.L.K.M.L.: Ãœber einen peptonartigen Bestandteil des Zellkerns. Z. Physiol. Chem. 8, 511 (1884).
Korinek, J., Spelsberg, T.C., Mitchell, W.M.: mRNA transcription linked to the morphological and plasma membrane changes induced by cyclic AMP in tumor cells. Nature 246, 455–458 (1973).
Lake, R.S., Goidl, J.A., Salzman, N.P.: F1 histone modification at metaphase in Chinese hamster cells. Exptl. Cell Res. 73, 113–121 (1972).
Lake, R.S., Salzman, N.P.: Occurance and properties of a chromatin associated F1 histone Phosphokinase in mitotic Chinese hamster cells. Biochemistry 11, 4817–4826 (1972).
Lake, R.S.: F1 histone phosphorylation in metaphase chromosomes of cultured Chinese hamster cels. Nature 24, 145–146 (1973).
Lake, R.S.: Further characterization of histone F1 Phosphokinase of metaphase arrested animal cells. J. Cel. Biol. 58, 317–331 (1973).
Lallier, R.: Effects of concanavalin A on the development of sea urchin egg. Exptl. Cell Res. 72, 157–163(1972).
Langan, T.: Histone phosphorylation: stimulation by adenosine 3′:5′ monophosphate. Science 162, 579–580 (1968).
Lawrence, D.J.R., Butler, J.A.V.: The metabolism of histones in malignant tissues and liver of rat and mouse. Biochem. J. 96, 53–62 (1965).
Lee, Y.C., Scherbaum, O.H.: Nucleohistone composition in stationary and division synchronized Tetrahymna cultures. Biochemistry 5, 2067–2075 (1966).
Lee, H.W., Paik, W.K., Borun, T.W.: The periodic synthesis of S-adenosylmethionine: protein methyltransferases during the Hela S-3 cell cycle. J. Biol. Chem. 248, 4149–4199 (1973).
LeStourgeon, W.M., Rusch, H.P.: Nuclear acidic protein changes during differentiation in Physarum polycephalum. Science 174, 1233–1236 (1971).
LeStourgeon, W.M., Rusch, H.P.: Localization of nucleolar ad chromatin residual acid protein changes during differentiatio in Physarum polycephalum. Arch. Biochem. Biophys. 155, 144–158 (1973).
Lindsay, D.T.: Histnes from developing tissues in the chicken: heterogeniety. Science 144,420–422(1964).
Lindsay, D.T.: Electrophoretically identical histones from the ribosomes and chromosomes of chicken liver. Arch. Biochem. Biophys. 113, 68–694 (1966).
Louie, A.J., Sung, M.T., Dixon, G.A.: Modification of histones during spermiogeesis in trout. III. Levels of phosphorylated species and kinetics of phosphorylation of histone. IIb. J. Biol. Chem. 248, 3335–3340 (1973).
Luck, J.M., Cook, H.A., Eldridge, N.T., Haley, M.I., Kupke, D.W., Rassmussen, P.S.: On the fractionation of calf thymus histones. Arch. Biochem. Biophys. 65, 449–467 (1956).
Luck, J.M., Rassmussen, P.S., Satake, K., Tsvetikov, A.N.: Further studies on the fractionation of calf thymus histone. J. Biol. Chem. 233 1407–1414 (1958).
Lynch, W.E., Brown, R.F., Umeda, T., Langreth, S., Lieberman, I.: Synthesis of deoxyribonucleic acid by isolated nuclei. J. Biol. Chem. 245, 3911–3916 (1970).
Maizel, J.V. Acrylamide gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins. Science 151, 990–998 (1967).
Malletti, L.A., Neblett, M., Exton, J.A., Langan, T.: Phosphorylation of lysine-rich histone in isoated perfused liver. J. Biol. Chem. 248, 6289–6291 (1973).
Marks, D., Paik, W.K., Borun, T.W.: The relationship of histone phosphorylation to deoxyribonucleic acid replication and mitosis during the Hela S-3 cell cycle. J. Biol. Chem. 248, 5660–5667 (1973).
Marzluff, W.F.; McCarty, K.S., Turkington, R.W.: Insulin dependent synthesis of histone in relation to the mammalian epithelial cell cycle. Biochim. iophys. Acta 190, 517–526(1969).
Mauritzen, C. W. M., Starbuck, W.C., Sarojal, S., Taylor, C.W., Busch, H.: The fractionation of arginine-rich histones from fetal calf thymus by exclusion chromatography. J. Biol. Chem. 242, 2240–2245 (1967).
McAllister, H.C., Jr., Wan, Y.C., Irvin, J.L.: Electrophoresis of histones and histone fractions on Polyacrylamide gels. Analyt. Biochem. 5, 321–329 (1963).
McLeish, J.: Comparative microphotometric studies of DNA and arginine in plant nuclei. Chromosoma 10, 686γ10 (1959).
MacGillivary, A.J.: The histones of some human tissues. Biochem. J. 110, 181–185 (1968).
Mirsky, A.E., Pollister, A.H.: Chromosin, a desoxyribonucleoprotein comples of the cell nucleus. J. Gen. Physiol. 30, 117–197 (p. 129) (1947).
Mirsky, A.E.: The structure of chromatin. Proc. Natl. Acad. Sci. U.S. 68, 2945–2948 (1971).
Mirsky, A.E., Silverma, N.B., Panda, N.: Blocking histones of the accesibility to DNA in chromatin: addition of histones. Proc. Natl. Acad. Sci. U.S. 69, 3243–3246 (1972).
Mirsky, A.E., Silverman, B.: The effect of selective extraction of histones on template activities of chromatin by use of exogenious DNA and RNA polymerases. Proc. Natl. Acad. Sci. U.S. 70, 1973–1975 (1973).
Mirsky, A. E.: Personal communication.
Moav, B., Nember, M.: Histone synthesis. Assignment to a special class of polyribosomes in sea urchin embryos. Biochemistry 10, 881–888 (1971).
Mohberg, J., Rusch, H.P.: Nuclear histones in Physarum polycephalum during growth and differentiation. Arch. Biochem. Biophys. 138, 418–432 (1970).
Mueller, G.C., Kajawara, K., Stubblefield, E., Rueckert, R.P.: Molecular events in the reproduction of animal cells. I. The effect of puromycin on the duplication of DNA. Cancer Res. 22, 1084–1090 (1962).
Murray, K.: The occurance of epsilon N-methyl lysine in histones. Biochemistry 3, 10–15(1964).
Murray, A.W., Froscio, M., Kemp, B.E.: Histone phosphotases and cyclic nucleotide stimulated protein kinase from human lymphocytes. Biochem. J. 129, 995–1002 (1972).
Neelin, J.M., Neelin, E.M.: Zone electrophoresis of calf thymus histones in starch gel. Canad. J. Biochem. Physiol. 38, 355–363 (1960).
Neelin, J.M., Butler, G.C.: A composition of histones from chicken tissues by zone electrophoresis in starch gel. Canad. J. Biochem. Physiol. 39, 485–491 (1961).
Callahan, P.X., Lamb, D.C., Murray, K.: The histones of chicken erythrocyte nuclei. Canad. J. Biochem. Physiol. 42, 1743–1752.
Neidle, A., Waelsch, H.: Histones: species and tissue specificity. Science 145, 420–422 (1964).
Nemer, M., Lindsay, D.T.: Evidence that S phase polysomes of early sea urchin embryos may be responsible for the synthesis of chromosomal proteins. 35, 156–160 (1969).
Oliver, D.R., Chalkley, R.: An electrophoretic analysis of Drosophila histones. Exptl. Cell Res. 73, 303–310 (1972).
Oliver, D.R., Balhorn, R., Granner, D., Chalkley, R.: Molecular nature of F1 histone phosphorylation in cultured hepatoma cells. Biochemistry 11, 3921–3915 (1972).
Ontko, J.A., Moorehead, W.R.: Histone synthesis after inhibition of deoxyribonucleic acid replication. Biochim. Biophys. Acta 91, 658–660 (1964).
Oppenheimer, B.S., Oppenheimer, E.T., Danishefsky, I., Stout, E.P., Eirich, F.R.: Further studies of polymers as carcinogenic agents in animals. Cancer Res. 15, 333–340 (1955).
Ord, M.G., Stocken, L.A.: Metabolic properties of histones from rat liver and thymus gland. Biochem. J. 98, 888–897 (1966).
Ord, M.G., Stocken, L.A.: Variations in the phosphate content and the thiol/disulfide ratio of histones during the cell cycle. Studies with regenerating rat liver and sea urchins. Biochem. J. 107, 403–410 (1968).
Ord, M.G., Stocken, L.A.: Further studies on the phosphorylation and the thiol/disulfide ratio of histones in growth and development. Biochem. J. 112, 81–89 (1969).
Paik, W.K., Kim, S.: Epsilon-N-dimethyllysine in histones. Biochem. Biophys. Res. Comm. 27, 479–483 (1967).
Paik, W.K., Kim, S.: Omega -n-methylarginine in histones. Biochem. Biophys. Res. Comm. 40, 224–229 (1970).
Paik, W.K., Kim, S.: Protein methylation. Science 174, 114–119 (1971).
Palau, J., Butler, J.A.V.: Trout liver histones. Biochem. J. 100, 779–783 (1966).
Painter, R.B., Schaefer, A.W.: The rate of synthesis along replicons of different kinds of mammalian cells. J. Molec. Biol. 45, 467–479 (1969).
Panyim, S., Chalkley, R.: High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. Biophys. 130, 337–346 (1969).
Panyim, S., Chalkley, R., Spiker, S., Oliver, D.: Constant electrophoretic mobility of the cysteine containing histone in plants and animals. Biochim. Biophys. Acta 214, 216–221 (1970).
Panyim, S., Bilek, D., Chalkley, R.: An electrophoretic comparison of vertebrate histories. J. Biol. Chem. 246, 4206–4215 (1971).
Paul, J., Gilmour, R.S.: Organ-specific restriction of transcription in mammalian chromatin. J. Molec. Biol. 34, 305–316 (1968).
Pawse, A.R., Ord, M.G., Stocken, L.A.: Histone kinase and cell division. Biochem. J. 122, 713–719 (1971).
Pederson, T., Robbins, E.: Absence of translational control of histone synthesis during the Hela cell cycle. J. Cell Biol. 45, 509–513 (1970).
Perry, R.P., Kelly, D.: Messenger RNA turnover in mouse L cells. J. Molec. Biol. 79, 681–696(1973).
Phillips, D.M.P.: The presence of acetyl groups in histones. Biochim. J. 87, 258–263 (1963).
Phillips, D.M.P., Johns, E.W.: A fractionation of histones of group F2a from calf thymus. Biochem. J. 94, 127–130 (1965).
Piha, R.S., Cuenod, M., Waelsch, H.: Metabolism of histones in liver and brain. J. Biol. Chem. 241, 2379–2404 (1966).
Pipkin, J.L., Larson, D.A.: Characterization of the very-lysine-rich histones of active and quiescent anther tissues of Hippeastrum belladonna. Exptl. Cell Res. 71, 249–260 (1972).
Pipkin, J.L., Larson, D.A.: Changing patterns of nucleic acid, basic and acidic proteins in generative and replicative nuclei during pollen germination and pollen tube formation in Hippeastrum belladonna. Exptl. Cell Res. 79, 28–42 (1973).
Platz, R.D., Hnilica, L.S.: Phosphorylation of non-histone chromatin proteins during sea urchin development. Biochem. Biophys. Res. Commun. 54, 222–227 (1973).
Prescott, D.M., Kimball, R.F.: Relation between RNA, DNA and protein synthesis in the replicating nucleus of Euplotes. Proc. Natl. Acad. Sci. U.S. 47, 686–693 (1961).
Prescott, D.M.: Regulation of cell reproduction. Cancer Res.28, 1815–1820 (1968).
Prescott, D.M.: Structure and reproduction of eucaryotic chromosomes. Advan. Cell Biol. 1, 57–117 (1970).
Prescott, D.M.: The synthesis of total macronuclear protein, histone and DNA during the cell cycle in Euplotes erystomus. J. Cell Biol. 31, 1–9 (1966).
Quagliarotti, G., Ogawa, Y., Taylor, C.W., Sautiere, P., Jordan, J.J., Starbuch, W.C., Busch, H.: Structural analysis of the glycine arginine rich histone. II. Sequence of the half of the molecule containing the aromatic amino acids. J. Biol. Chem. 244, 1796–1802(1969).
Raff, R.A.: Polar lobe formation by embryos of Ilyanassa obsoleta. Exptl. Cell Res. 71, 455–459 (1972).
Ranieri, R., Simeiaman, G., Boutwell, R.K.: Stimulation of the phosphorylation of mouse epidermal histones by tumor promoter agents. Cancer Res.33, 134–139 (1973).
Rasmussen, P.S., Murray, K., Luck, J.M.: On the complexity of calf thymus histones. Biochemistry 1, 79–89 (1962).
Raymond, S., Weintraub, L.: Acrylamide gel as a supporting medium for zone electrophoresis. Science 130, 711 (1959).
Reichman, M., Penman, S.: Stimulation of polypeptide initiation in vitro in Hela cells. Proc. Natl. Acad. Sci. U.S. 70, 2678–2682 (1973).
Roberts, J.H., Stark, P., Smulson, M.: Stimulation of DNA synthesis by adenosine diphosphoribosylation of Hela nuclear proteins during the cell cycle. Biochem. Biophys. Res. Commun. a52, 43–50 (1973).
Robbins, E., Borun, T.W.: The cytoplasmic synthesis of histones in Hela cells and its temporal relationship to DNA replication. Proc. Natl. Acad. Sci. U.S. 57, 409–416 (1967).
Rudderman, J.V., Baglioni, C., Croso, T.R.: Histone mRNA and histone synthesis during embryogenesis. Nature 247, 36–37 (1974).
Sadgopal, A., Bonner, J.: The relationship between histone and DNA synthesis in Hela cells. Biochim. Biophys. Acta 186, 349–357 (1969).
Sanger, R., Lane, D.: Molecular basis of maternal inheritance. Proc. Natl. Acad. Sci. U.S. 69, 2410–2413 (1972).
Sautiere, P., Starbuck, W.C., Roth, C., Busch, H.: Structural analysis of the glycine-arginine rich histone (f2a1). I. Sequence of the carboxyl terminal portion. J. Biol. Chem. 243,319–334(1968).
Sautiere, M.P., Tyrou, D., Laine, B., Mizon, J., Lambetin-Breynaert, M.D., Ruggin, P., Biserte, D.: Structure primaire de l’histone riche en arginine et en lysine du thymus de veau. Compt. Rend. 274, 1422 (1972).
Schochetman, G., Perry, R.P.: Early appearance of histone messenger RNA in polyribosomes of cultured L cells. J. Molec. Biol. 63 591–596 (1972).
Seale, R.L., Aronson, A.I.: Chromatin associated proteins of the developing sea urchin embryo. I. The kinetics of synthesis and characterization of nonhistone proteins. J. Molec. Biol. 75, 633–645 (1973).
Seale, R.L., Aronson, A.I.: Chromatin associated proteins of the developing sea urchin embryo. II. Acid-soluble proteins. J. Molec. Biol. 5, 647–658 (1973).
Seed, J.: The synthesis of DNA, RNA and nuclear protein in normal and tumor strain cells. I. Fresh embryo cells from humans. J. Cell Biol. 28, 233–248 (1966).
Seed, J.: The synthesis of DNA, RNA and nuclear protein in normal and tumor strain cells. II. Fresh embryo mouse cells. J. Cell Biol. 28, 249–256 (1966).
Shapiro, A.L., Vinuela, E., Maizel, J.V.,Jr.: Molecular weight estimations of polypeptide chains by electrophoresis in SDS Polyacrylamide gels. Biophys. Biochem. Res. Commun. 28, 815–820 (1967).
Shapiro, I.M., Levina, L.Y.: Autoradiographic study on the time of nuclear protein synthesis in human leukocyte blood culture. Exptl. Cell Res. 47, 75–85 (1967).
Shapiro, I.M., Levina, L.Y.: Incorporation of proteins labeled with 3H-lysine into chromosomes of human leukocytes cultures in vitro. Chromosoma 25, 30 (1968).
Sherod, D., Johnson, G., Chalkley, R.: Phosphorylation of mouse ascites tumor cell lysine-rich histone. Biochemistry 9, 4611–4615 (1970).
Shepherd, G.R., Hardin, J.M., Noland, B.J.: Methylation of lysine residues in histone fractions in synchronized mammalian cells. Arch. Biochem. Biophys. 143, 1–5 (1971).
Siebert, G., Ord, M.G., Stocken, L.A.: Histone Phosphokinase activity in nuclear and cytoplasmic cell fractions from normal and regenerating rat liver. Biochem. J. 122, 721–725 (1971).
Silverman, B., Mirsky, A.E.: Addition of histones to histone depleated nuclei: effect on template activity towards DNA and RNA polymerases. Proc. Natl. Acad. Sci. U.S. 70, 2637–2641 (1973).
Simpson, R.T., Reeck, G.R.: A comparison of the proteins of condensed and extended chromatin fractions of rabbit liver and calf thymus. Biochemistry 12, 3853–3858 (1973).
Skoultchi, A., Gross, P.R.: Maternal histone messenger RNA: detection by molecular hybridization. Proc. Natl. Acad. Sci. U.S. 70, 2840–2844 (1973).
Smith, J.A., Stocken, L.A.: Characterization of a non-histone protein isolated from histone F1 preparations. Biochem. J. 131, 859–861 (1973).
Smith, J.A., Stocken, L.A.: Identification of poly (ADPR) convalently bound to histone F1 in vivo. Biochem. Biophys. Res. Commun. 54, 297–300 (1973).
Solomos, T., Laties, G.G.: Cellular organization and fruit ripening. Nature 245, 390–392 (1973).
Sonnenberg, B.P., Zubay, G.: Nucleohistone as primer for RNA synthesis. Proc. Natl. Acad. Sci. U.S. 54, 415–420 (1965).
Spaulding, J., Kajiwara, K., Mueller, G.C.: The metabolism of basic proteins in Hela cell nuclei. Proc. Natl. Acad. Sci. U.S. 56, 1535–1542 (1966).
Stedman, E., Stedman, E.: Cell specificity of histones. Nature 166, 780–781 (1950).
Stedman, E., Stedman, E.: The basic proteins of cell nuclear. Phil. Trans. Roy. Soc. B 235, 565 (1957).
Stein, G.S., Borun, T.W.: The synthesis of acidic chromosomal proteins during the cell cycle of Hela S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication. J. Cell Biol. 52, 292–307 (1972).
Stellwagen, R.H., Cole, R.D.: Danger of contamination in chromatographically prepared arginine-rich histones. J. Biol. Chem. 243, 4452–4455 (1968).
Stellwagen, R.H., Cole, R.D.: Comparison of histones obtained from mammary gland at different stages of development and lactation. J. Biol. Chem. a243, 4456–4462 (1968).
Stellwagen, R.H., Cole, R.D.: Chromosomal proteins. Ann. Rev. Biochem. 38, 951—990(1969).
Stellwagen, R.H., Cole, R.D.: Histone biosynthesis in the mammary gland during development and lactation. J. Biol. Chem. 244, 4878–4887 (1969).
Stevely, W.S., Stocken, L.A.: Variations in phosphate content in histone F1 in normal and irradiated tissues. Biochemistry J. 110, 187–191 (1968).
Stout, J.T., Phillips, R.L.: Two independently inhibited electrophorietic varients of the lysine-rich histones of Maize (Zea mays). Proc. Natl. Acad. Sci. U.S. 70, 3043–3047 (1973).
Subirana, J.A., Palau, J., Cozeolluella, C., Ruiz-Canilo, A.: Very lysine rich histone of echinoderms and molluscs. Nature 228, 992–993 (1970).
Summerbell, D., Leivis, J.H., Wolpert, L.: Postitional information in chick limb morphogenesis. Nature 244, 492–496 (1973).
Swift, H.: The constancy of desoxyribosenucleic acid in plant nuclei. Proc. Natl. Acad. Sci. U.S. 36, 643–653 (1950).
Szyan, I., Burdman, J. A.: The relationship between DNA synthesis and the synthesis of nuclear proteins in rat brain. Effect of hydrocortisone acetate. Biochim. Biophys. Acta 299, 294–353 (1973).
Takai, S., Borun, T.W., Muchmore, J., Lieberman, I.: Concurrent synthesis of histone and desoxyribonucleic acid in liver after partial hepatectomy. Nature 219, 860–861 (1968).
Teller, D.C., Kinkade, J.M., Cole, R.D.: The molecular weight of lysine-rich histone. Biophys. Biochem. Res. Commun. 20 739–744 (1965).
Tidwell, T., Allfrey, V.G., Mirsky, A.E.: The methylation of histones during regeneration of the liver. J. Biol. Chem. 243, 707–715 (1968).
Tomkins, G.M., Gelehrter, T.P., Granner, D., Martin, D., Samuels, H.A., Thompson, E.B.: Control of specific gene expressions in higher organisms. Science 166, 1474–1480(1969).
Umana, R., Updike, S., Randall, J., Dounce, A.L.: Histone metabolism. In: The Nu-cleoproteins (Bonner, T’so, Eds.). San Francisco: Holden-Day 1964.
Vidali, G., Gershey, E.L., Allfrey, V.G.: Chemical studies of histone acetyllation. The occurance of epsilon-N-acetyllysine in calf thymus histone. J. Biol. Chem. 243, 6361–6366(1968).
Vidali, G., Boffa, L.C., Allfrey, V.G.: Properties of an acidic histone-binding protein fraction from cell nuclei. Selective precipitation and deacetylation of histones F2al and F3. J. Biol. Chem. 247, 7365–7373 (1972).
Wasserman, G.B.: Molecular genetics and developmental biology. Nature 245, 163–165 (1973).
Weber, K., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406–4412 (1969).
Weinberg, E.S., Birnstiel Purdom, I.F., Williamson, R.: Genes coding for polyribo-somal 9S RNA of sea urchins: conservation divergence. Nature 240, 449–453 (1972).
Weintraub, H.: A possible role for histone in the synthesis of DNA. Nature 240, 449–453 (1972).
Wessels, N.K., Sponner, B.S., Ash, J.F., Bradley, M.O., Luduena, M.A., Taylor, E.L., Wrenn, J.T., Yamada, K.M.: Microfiliments in developmental processes. Science 171, 135–143 (1971).
Whittaker,J.R.: Segregation during ascidian embryogenesis of egg cytoplasmic information for tissue-specific enzyme development. Proc. Natl. Acad. Sci. U.S. 2096–2100 (1973).
Williamson, D.H.: Replication of the nuclear genome in yeast does not require concurrent protein synthesis. Biochem. Biophys. Res. Commun. 52, 731–740 (1973).
Wolpert, L., Clarke, M.R.B., Hornbruch, A.: Positional signalling along Hydra. Nature 239, 101–105 (1972).
Woodward, J., Rasch, E., Swift, H.: Nucleic acid and protein metabolism during the mitotic cycle in Viva faba. J. Biophys. Biochem. Cytol. 9, 445–462 (1960).
Yamada, M, Sugimura, T.: Effects of deoxyribonucleic acid and histone on number and length of chains of poly ADPR. Biochemistry 12, 3303–3308 (1973).
Yarbro, J.W., Niehaus, W.G., Barnum, C. P.: Effect of hydroxyurea on regenerating rat liver. Biochem. Biophys. Res. Commun. 19, 592–597 (1965).
Zauderer, M., Liberti, P., Baglioni, C.: Distribution of histone messenger RNA among free and membrane-bound polyribosomes of a mouse myeloma line. J. Molec. Biol. 79, 577–586 (1973).
Zampetti-Bosseler, F., Malpoix, P., Fievez, M.: Differential inhibition of protein synthesis in the nucleus and cytoplasm of Hela cells in the presence of actinomycin, puromycin and hydroxyurea. European J. Biochem. 9, 21–26 (1969).
Zubay, G. (Ed.): Papers in Biochemical Genetics. First Ed., p.466. New York: Holt, Rienhart and Winston 1968.
Zweidler, F.: Strukturen und Replication der Chromosomen. Ph. D. thesis. Universität Zürich: Truninger Druckanstalt 1965.
Zwiedler, A., Borun, T.W.: In preparation (1974).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1975 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Borun, T.W. (1975). Histones, Differentiation, and the Cell Cycle. In: Reinert, J., Holtzer, H. (eds) Cell Cycle and Cell Differentiation. Results and Problems in Cell Differentiation, vol 7. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-37390-2_12
Download citation
DOI: https://doi.org/10.1007/978-3-540-37390-2_12
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-21693-4
Online ISBN: 978-3-540-37390-2
eBook Packages: Springer Book Archive