Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 May;78(5):2874–2878. doi: 10.1073/pnas.78.5.2874

Assessment of estrogen receptor--histone interactions.

J Kallos, T M Fasy, V P Hollander
PMCID: PMC319461  PMID: 6942408

Abstract

Several different in vitro binding assays show that the estrogen receptor from rabbit uterus interacts selectively with purified histones from calf thymus. The estrogen receptor binds strongly to histones H2B and H2A, moderately to histones H3 and H4, and poorly to histone H1. In the presence of histones H2B or H2A, the position at which the estrogen receptor focuses in an isoelectric gradient is shifted to a more basic zone. Kinetic experiments show that, if histone H2B is bound to a DNA, the estrogen receptor dissociates more slowly from that DNA. The portion of the estrogen receptor molecule required for binding to histone H2B is relatively stable to tryptic digestion; in contrast, the portion of the receptor molecule responsible for DNA binding is promptly lost during limited tryptic digestion. These in vitro findings suggest that the mechanism by which the estrogen receptor selectively alters gene expression may involve specific contacts with histone molecules.

Full text

PDF
2874

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andre J., Raynaud A., Rochefort H. Characterization of the estradiol receptor extracted from nuclei by micrococcal nuclease. Biochemistry. 1978 Aug 22;17(17):3619–3626. doi: 10.1021/bi00610a031. [DOI] [PubMed] [Google Scholar]
  2. Andre J., Rochefort H. Estrogen receptor: loss of DNA binding ability following trypsin or Ca2+ treatment. FEBS Lett. 1973 Jun 1;32(2):330–334. doi: 10.1016/0014-5793(73)80866-x. [DOI] [PubMed] [Google Scholar]
  3. Böhm E. L., Strickland W. N., Strickland M., Thwaits B. H., van der Westhuizen D. R., von Holt C. Purification of the five main calf thymus histone fractions by gel exclusion chromatography. FEBS Lett. 1973 Aug 15;34(2):217–221. doi: 10.1016/0014-5793(73)80797-5. [DOI] [PubMed] [Google Scholar]
  4. Chamness G. C., Huff K., McGuire W. L. Protamine-precipitated estrogen receptor: a solid-phase ligand exchange assay. Steroids. 1975 May;25(5):627–635. doi: 10.1016/0039-128x(75)90017-3. [DOI] [PubMed] [Google Scholar]
  5. Clark J. H., Peck E. J. Nuclear retention of receptor-oestrogen complex and nuclear acceptor sites. Nature. 1976 Apr 15;260(5552):635–637. doi: 10.1038/260635a0. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Feldman M., Kallos J., Hollander V. P. Effect of photooxidation on the estrogen receptor from rat mammary tumor. J Biol Chem. 1980 Sep 25;255(18):8776–8779. [PubMed] [Google Scholar]
  8. Garel A., Axel R. Selective digestion of transcriptionally active ovalbumin genes from oviduct nuclei. Proc Natl Acad Sci U S A. 1976 Nov;73(11):3966–3970. doi: 10.1073/pnas.73.11.3966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gorski J., Gannon F. Current models of steroid hormone action: a critique. Annu Rev Physiol. 1976;38:425–450. doi: 10.1146/annurev.ph.38.030176.002233. [DOI] [PubMed] [Google Scholar]
  10. Isenberg I. Histones. Annu Rev Biochem. 1979;48:159–191. doi: 10.1146/annurev.bi.48.070179.001111. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Kallos J., Fasy T. M., Hollander V. P., Bick M. D. Estrogen receptor has enhanced affinity for bromodeoxyuridine-substituted DNA. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4896–4900. doi: 10.1073/pnas.75.10.4896. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. King R. J., Gordon J., Steggles A. W. The properties of a nuclear acidic protein fraction that binds [6,7-3H]oestradiol-17beta. Biochem J. 1969 Sep;114(3):649–657. doi: 10.1042/bj1140649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. 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]
  17. March S. C., Parikh I., Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem. 1974 Jul;60(1):149–152. doi: 10.1016/0003-2697(74)90139-0. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. PHILLIPS D. M., JOHNS E. W. A FRACTIONATION OF THE HISTONES OF GROUP F2A FROM CALF THYMUS. Biochem J. 1965 Jan;94:127–130. doi: 10.1042/bj0940127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. Puca G. A., Nola E., Hibner U., Cicala G., Sica V. Interaction of the estradiol receptor from calf uterus with its nuclear acceptor sites. J Biol Chem. 1975 Aug 25;250(16):6452–6459. [PubMed] [Google Scholar]
  22. Puca G. A., Sica V., Nola E. Identification of a high affinity nuclear acceptor site for estrogen receptor of calf uterus. Proc Natl Acad Sci U S A. 1974 Mar;71(3):979–983. doi: 10.1073/pnas.71.3.979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ratajczak T., Hähnel R. Chromatographic and other properties of the estrogen receptors from human myometrium. J Steroid Biochem. 1976 Mar;7(3):185–197. doi: 10.1016/0022-4731(76)90201-6. [DOI] [PubMed] [Google Scholar]
  24. Rochefort H., André J., Baskevitch P. P., Kallos J., Vignon F., Westley B. Nuclear translocation and interactions of the estrogen receptor in uterus and mammary tumors. J Steroid Biochem. 1980 Jan;12:135–142. doi: 10.1016/0022-4731(80)90263-0. [DOI] [PubMed] [Google Scholar]
  25. Ruiz-Carrillo A., Allfrey V. G. A method for the purification of histone fraction F3 by affinity chromatography. Arch Biochem Biophys. 1973 Jan;154(1):185–191. doi: 10.1016/0003-9861(73)90047-7. [DOI] [PubMed] [Google Scholar]
  26. Ruiz-Carrillo A., Wangh L. J., Littau V. C., Allfrey V. G. Changes in histone acetyl content and in nuclear non-histone protein composition of avian erythroid cells at different stages of maturation. J Biol Chem. 1974 Nov 25;249(22):7358–7368. [PubMed] [Google Scholar]
  27. Senior M. B., Frankel F. R. Evidence for two kinds of chromatin binding sites for the estradiol-receptor complex. Cell. 1978 Aug;14(4):857–863. doi: 10.1016/0092-8674(78)90341-0. [DOI] [PubMed] [Google Scholar]
  28. Simons S. S., Jr Factors influencing association of glucocorticoid receptor-steroid complexes with nuclei, chromatin, and DNA: interpretation of binding data. Monogr Endocrinol. 1979;12:161–187. doi: 10.1007/978-3-642-81265-1_9. [DOI] [PubMed] [Google Scholar]
  29. Simons S. S., Jr, Martinez H. M., Garcea R. L., Baxter J. D., Tomkins G. M. Interaction of glucocorticoid receptor-steroid complexes with acceptor sites. J Biol Chem. 1976 Jan 25;251(2):334–343. [PubMed] [Google Scholar]
  30. Sluyser M. Interaction of steroid hormones with histones in vitro. Biochim Biophys Acta. 1969 May 20;182(1):235–244. doi: 10.1016/0005-2787(69)90538-3. [DOI] [PubMed] [Google Scholar]
  31. Sluyser M. Mechanism of action of cortisol in rat liver. Biochem J. 1972 Nov;130(2):49P=–450P. doi: 10.1042/bj1300049p. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Spelsberg T. C., Webster R., Pikler G., Thrall C., Wells D. Nuclear binding sites ("acceptors") for progesterone in avian oviduct: characterization of the highest-affinity sites. Ann N Y Acad Sci. 1977 Mar 11;286:43–63. doi: 10.1111/j.1749-6632.1977.tb29404.x. [DOI] [PubMed] [Google Scholar]
  33. Steggles A. W., King R. J. The use of protamine to study [6,7-3H] oestradiol-17-beta binding in rat uterus. Biochem J. 1970 Aug;118(5):695–701. doi: 10.1042/bj1180695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Sunaga K., Koide S. S. Structural specificity of the steroids interacting with calf thymus histones. Biochem Biophys Res Commun. 1967 Feb 8;26(3):342–348. doi: 10.1016/0006-291x(67)90129-5. [DOI] [PubMed] [Google Scholar]
  35. Thanki K. H., Beach T. A., Bass A. I., Dickerman H. W. Stimulation of oligonucleotide binding of estradiol receptor complexes by accessory proteins. Nucleic Acids Res. 1979 Aug 24;6(12):3859–3877. doi: 10.1093/nar/6.12.3859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Toft D. The interaction of uterine estrogen receptors with DNA. J Steroid Biochem. 1972 Apr;3(3):515–522. doi: 10.1016/0022-4731(72)90098-2. [DOI] [PubMed] [Google Scholar]
  37. Tsai Y. H., Hnilica L. S. Interactions of histones with corticosteroid hormones. Biochim Biophys Acta. 1971 May 13;238(2):277–287. doi: 10.1016/0005-2787(71)90094-3. [DOI] [PubMed] [Google Scholar]
  38. 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]
  39. 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]
  40. Yamamoto K. R., Alberts B. On the specificity of the binding of the estradiol receptor protein to deoxyribonucleic acid. J Biol Chem. 1974 Nov 25;249(22):7076–7086. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES