Summary
Histones were extracted from leaves of winter- and spring-wheat seedlings, flowering shoots of spring wheat, shoots of vernalized and control winter wheat, and roots and shoots of winter wheat, and were compared by polyacrylamide-gel electrophoresis. No differences were found either in the electrophoretic mobility or relative quantity of the various fractions. Wheat histones contained fractions of the exact electrophoretic mobility as F2a1 and F3 of calf thymus and pea histones. Other major fractions of the wheat histones had electrophoretic mobilities similar to those of F1, F2b and F2a2 of peas.
This is a preview of subscription content, log in via an institution to check access.
References
Allfrey, V. G., Littau, V. C., Mirsky, A. E.: On the role of histones in regulating ribonucleic acid synthesis in the cell nucleus. Proc. nat. Acad. Sci. (Wash.) 49, 414–421 (1963).
Balhorn, R., Chalkley, R., Granner, D.: Lysine-rich histone phosphorylation. A positive correlation with cell replication. Biochemistry 11, 1094–1098 (1972).
Bonner, J.: The role of histones in the regulation of RNA synthesis. In: Regulation of nucleic acid and protein biosynthesis, p. 211–224 (Konigsberger, V. V., Bosch, L., eds.). Amsterdam: Elsevier 1967.
Bonner, J., Chalkley, G. R., Dahmus, M., Fambrough, D., Fujimura, F., Huang, R. C., Huberman, J., Jensen, R., Marushige, K., Ohlenbusch, H., Olivera, B., Widholm, J.: Isolation and characterization of chromosomal nucleoproteins. In: Methods in enzymology (nucleic acids), vol. 12b, p. 3–65 (Grossman, L., Moldave, K., eds.). New York: Acad. Press 1968.
Cohn, N. S., Quatrano, P. S.: Extraction and analysis of histone protein from the roots of three plant species. Experientia (Basel) 21, 237–240 (1965).
DeLange, R. J., Fambrough, D. M., Smith, E. L., Bonner, J.: Calf and pea histone IV. J. biol. Chem. 244, 5669–5679 (1969).
DeLange, R. J., Smith, E. L.: Histones: structure and function. Ann. Rev. Biochem. 40, 279–314 (1971).
Fambrough, D. M., Bonner, J.: Sequence homology and role of cysteine in plant and animal arginine-rich histones. J. biol. Chem. 243, 4434–4439 (1968).
Fambrough, D. M., Fujimura, F., Bonner, J.: Quantitative distribution of histone components in the pea plant. Biochemistry 7, 575–585 (1968).
Georgiev, G. P.: Histones and the control of gene action. Ann. Rev. Genet. 3, 155–180 (1969).
Gutierrez, R. M., Hnilica, L. S.: Tissue specificity of histone phosphorylation. Science 157, 1324–1325 (1967).
Hnilica, L. S., Johns, E. W., Butler, J. A. V.: Observations of the species and tissue specificity of histones. Biochem. J. 82, 123–129 (1962).
Jacobson, R. A., Bonner, J.: Studies of the chromosomal RNA and of the chromosomal RNA binding protein of higher organisms. Arch. Biochem. 146, 557–563 (1971).
Johns, E. W.: Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem. J. 92, 55–59 (1964).
Mauritzen, C. M., Stedman, E.: Cell specificity of B-histones in the domestic fowl. Proc. roy. Soc. B 150, 299–311 (1959).
Oliver, D., Sommer, K., Panyim, S., Spiker, S., Chalkley, R.: A modified technique of histone fractionation. Biochem. J. 129, 349–353 (1972).
Panyim, S., Bilek, D., Chalkley, R.: An electrophoretic comparison of vertebrate histones. J. biol. Chem. 246, 4206–4215 (1971a).
Panyim, S., Chalkley, G. R.: High resolution acrylamide gel electrophoresis of histones. Arch. Biochem. 130, 337–346 (1969a).
Panyim, S., Chalkley, R.: The heterogeneity of histones. I. A quantitative analysis of calf thymus histones in very long polyacrylamide gels. Biochemistry 8, 3972–3979 (1969b).
Panyim, S., Chalkley, R., Spiker, S., Oliver, D.: Constant electrophoretic mobility of the cysteine-containing histone in plants and animals. Biochim. biophys. Acta (Amst.) 214, 216–221 (1970).
Panyim, S., Jensen, R. H., Chalkley, G. R.: Proteolytic contamination of calf thymus nucleohistone and its inhibition. Biochim. biophys. Acta (Amst.) 160, 252–255 (1968).
Panyim, S., Sommer, K., Chalkley, R.: Oxidation of the cysteine-containing histone F3. Detection of an evolutionary mutation in a conservative histone. Biochemistry 10, 3911–3917 (1971b).
Pipkin, J. L., Larson, D. A.: Characterization of the “very” lysine-rich histones of active and quiescent anther tissues of Hippeastrum belladonna. Exp. Cell Res. 71, 249–260 (1972).
Pogo, B. G. T., Pogo, A. O., Allfrey, V. G., Mirsky, A. E.: Changing patterns of histone acetylation and RNA synthesis in regeneration of the liver. Proc. nat. Acad. Sci. (Wash.) 59, 1337–1344 (1968).
Snedecor, G. W., Cochran, W. G.: Statistical methods. Ames: Iowa State Univ. Press 1971.
Spiker, S.: The relationship of histones to plant growth and development. Doct. dissert., Univ. of Iowa. Iowa City, 1970.
Spiker, S., Chalkley, R.: Electrophoretic analysis of histones from gibberellic acid. treated dwarf peas. Plant Physiol. 47, 342–345 (1971).
Stedman, E., Stedman, E.: Cell specificity of histones. Nature (Lond.) 166, 780 (1950).
Teng, C. S., Teng, C. T., Allfrey, V. G.: Studies of nuclear acidic proteins. J. biol. Chem. 246, 3597–3609 (1971).
Teraoka, H.: Proteins of wheat embryos in the period of vernalization. Plant & Cell Physiol. 8, 87–95 (1967).
Teraoka, H.: Histones of wheat embryos during the period of vernalization. Plant & Cell Physiol. 9, 819–823 (1968).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Spiker, S., Krishnaswamy, L. Constancy of wheat histones during development. Planta 110, 71–76 (1973). https://doi.org/10.1007/BF00386924
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00386924