Skip to main content

The Structures and Functions of the Low Molecular Weight HMG Proteins

  • Chapter
Book cover Chromosomal Proteins and Gene Expression

Part of the book series: NATO ASI Series ((NSSA,volume 101))

Abstract

It is a widely held view that during the development of an organism genes that are to be activated in a particular cell type are assembled in a specific chromatin structure prior to the onset of transcription. Considerable effort has been devoted to elucidating the components of such “transcriptionally competent” chromatin. Evidence that active genes have a different chromatin structure from inactive genes has come from nuclease digestion experiments. In such experiments it has been found that all active genes or potentially active genes are very much more sensitive to digestion by DNase I than inactive genes. This sensitivity was primarily attributed to an altered core particle structure of the nucleosomes bound to active genes (1). The discovery that the small HMG proteins*, HMG-14 and HMG-17, could induce such a conformational change in nucleosomes (2) raised the possibility that the structural alterations that occur in nucleosomes prior to or during transcription could be analysed in detail.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. WEINTRAUB, H. and GROUDINE, M. (1976). Chromosomal subunits in active genes have an altered conformation. Science 193, 848–858.

    Article  PubMed  CAS  Google Scholar 

  2. la. JOHNS, E.W., ed. (1983). “The HMG Chromosomal Proteins.” Academic Press, New York.

    Google Scholar 

  3. WEISBROD, S., GROUDINE, M., and WEINTRAUB, H. (1980). Interaction of HMG14 and 17 with actively transcribed genes. Cell 19, 289–299.

    Article  PubMed  CAS  Google Scholar 

  4. GOODWIN, G.H., NICOLAS, R.H., and JOHNS, E.W. (1975). An improved large scale fractionation of high mobility group non-histone chromosomal proteins. Biochim. Biophys. Acta 405, 280.

    Google Scholar 

  5. GOODWIN, G.H., RABBANI, A., NICOLAS, R.H., and JOHNS, E.W. (1977). The isolation of the high mobility group nonhistone chromosomal protein HMG-14. FEBS Lett. 80, 413–416.

    Article  PubMed  CAS  Google Scholar 

  6. LUND, I., HOLTLUND, J., FREDRIKSEN, M., and LALAND, S. (1983). On the presence of two new high mobility group-like proteins in HeLa S3 cells. FEBS Lett. 152, 163–167.

    Article  PubMed  CAS  Google Scholar 

  7. GOODWIN, G.H., BROWN, E., WALKER, J.M., and JOHNS, E.W. (1980). The isolation of three new HMG nuclear proteins. Biochim. Biophys. Acta 623, 329–338.

    Google Scholar 

  8. WALKER, J.M. (1982). Primary structures. In: “The HMG Chromosomal Proteins,” (E.W. Johns, ed.) pp.-b9–87. Academic Press, New York.

    Google Scholar 

  9. NICOLAS, R.H. and GOODWIN, G.H. (1982). Isolation and analysis. In: “The HMG Chromosomal Proteins” (E.W. Johns, ed.) pp. 417T8. Academic Press, New York.

    Google Scholar 

  10. WEN, L., TWETEN, R.K., ISACKSON, P.J., IANDOLO, J.J., and REECK, G.R. (1983). Ionic interacctions between proteins in non-equilibrium pH gradient electrophoresis. Anal. Biochem. 132, 294–304.

    Google Scholar 

  11. GOODWIN, G.H., WRIGHT, C.A., and JOHNS, E.W. (1981). The characterization of ISF monomer nucleosomes from hen oviduct and the partial characterization of a third HMG-14/17like protein in such nucleosomes. Nucleic Acids Res. 9, 2761–2775.

    Article  PubMed  CAS  Google Scholar 

  12. RABBANI, A., GOODWIN, G.H., WALKER, J.M., BROWN, E., and JOHNS, E.W. (1980). Trout liver high mobility group non-histone chromosomal proteins. FEBS Lett. 109, 294–398.

    Article  PubMed  CAS  Google Scholar 

  13. WATSON, D.C., WONG, N.C.W., and DIXON, G.H. (1979). The complete amino acid sequence of a trout testis non-histone protein H6 localised in a subset of nucleosomes and its similarity to calf thymus non-histone proteins HMG14 and HMG17. Eur. J. Biochem. 95, 193–199.

    Google Scholar 

  14. WALKER, J. M., HASTINGS, J. R. B., and JOHNS, E. W. (1977). The primary structure of a non-histone chromosomal protein. Eur. J. Biochem. 76 461–468.

    Google Scholar 

  15. WALKER, J.M., GOODWIN, G.H., and JOHNS, E.W. (1979). The primary structure of the nucleosome-associated chromosomal protein HMG-14. FEBS Lett. 100, 394–399.

    Article  PubMed  CAS  Google Scholar 

  16. WALKER, J.M., BROWN, E., GOODWIN, G.H., STEARN, C., and JOHNS, E.W. (1980). Studies on the structures of some HMG-like non-histone chromosomal proteins from trout and chicken tissues comparison with calf thymus proteins HMG-14 and 17. FEBS Lett. 113, 253–257.

    Article  PubMed  CAS  Google Scholar 

  17. SAFFER, J.D. and GLAZER, R.I. (1982). The phosphorylation of high mobility group proteins HMG-14 and 17 and their distribution in chromatin. J. Biol. Chem. 257, 4655–4660.

    Google Scholar 

  18. COOPER, E. and SPAULDING, S.W. (1983). HMG-14/17-like proteins in calf thyroid. Biochem. J. 215, 643–649.

    Google Scholar 

  19. WALTON, G.M., GILL, G.H., COOPER, E., and SPAULDING, S.W. (1984). Thyrotropin-stimulated phosphorylation of high-mobility group protein 14 in vivo at the site catalysed by cyclic nucleoside-dependent protein kinases in vitro. J. Biol. Chem. 259, 601–607.

    Google Scholar 

  20. REECK, G.R. and TELLER, D.C. (1985) proteins: purification, properties quence comparisons. In: “Progress Research,” Vol. II ( I Bekhor, ed.) Boca Raton, Florida.

    Google Scholar 

  21. WALTON, G.M. and GILL, G.H. (1983). Identity of the in vivo phosphorylation site in high mobility group 14 protein in HeLa cells with the site phosphorylated by casein kinase II in vitro.J. Biol. Chem. 258 4440–4446.

    Google Scholar 

  22. LUND, T., HOLTLUND, J., KRISTENSEN, T., OSTVOLD, A.C., SLETTEN, K., and LALAND, S.G. (1981). HMG-17 in metaphase arrested and interphase HeLa S3 cells. FEBS Lett. 133, 8489.

    Article  Google Scholar 

  23. D’ANNA, J.A., BECKER, R.R., TOBEY, R.A., and GATHEY, L.R. (1983). Composition and synthesis during G and S phase of a high mobility group-E/G component from Chinese hamster ovary cells. Biochim. Biophys. Acta 739, 197–206.

    Google Scholar 

  24. ALLFREY, V.G. (1982). Postsynthetic modifications. In: “The HMG Chromosomal Proteins, ( E.W. Johns, ed.) pp. 1148. Academic Press, New York and London.

    Google Scholar 

  25. DIXON, G.H. (1978). The HMG proteins of rainbow trout testis nuclei: isolation, structure, and function. In: “The HMG Chromosomal Proteins,” (E.W. Johns, ed.) pp. M-192. Academic Press, New York and London.

    Google Scholar 

  26. TANUMA, S., JOHNSON, L.D., and JOHNSON, G.S. (1983). ADP-ribosylation of chromosomal proteins and mouse mammary tumour virus gene expression. J. Biol. Chem. 258, 15371–15375.

    Google Scholar 

  27. RING, D. and COLE, R. D. (1979). Chemical cross-linking of H1 histone to the nucleosomal histone. J. Biol. Chem. 254, 11688–11695.

    Google Scholar 

  28. GAZIT, B., PANET, A., and CEDAR, H. (1980). Reconstitution of a deoxyribonuclease I-sensitive strucure on active genes. Proc. Natl. Acad. Sci. 77, 1787–1790.

    Google Scholar 

  29. WEISBROD, S. and WEINTRAUB, H. (1981). Isolation of activity of transcribed nucleosomes using immobilized HMG-14 and HMG-17 and an analysis of a-globin chromatin. Cell 23, 391–401.

    Article  PubMed  CAS  Google Scholar 

  30. LEVY, W.B. and DIXON, G.H. (1978). Partial purification of transcriptionally active nucleosomes from trout testis cells. Nucleic Acids Res. 5, 4155–4167.

    Article  PubMed  CAS  Google Scholar 

  31. GOODWIN, G.H. and MATHEW, C.G.P. (1982). Role in gene structure and function. In: “The HMG Chromosomal Proteins,” ( E.W. Johns, ed.) pp. 193–221. Academic Press, New York.

    Google Scholar 

  32. NICOLAS, R.H., WRIGHT, C.A., COCKERILL, P.N., WYKE, J.A., and GOODWIN, G.H. (1983). The nuclease sensitivity of active genes. Nucleic Acids Res 753–772.

    Article  PubMed  CAS  Google Scholar 

  33. BARSOUM, J., LEVINGER, L., and VARSHAVSKY, A. (1982). On the chromatin structure of the amplified, transcriptionally active gene for dihydrofolate reductase in mouse cells. J. Biol. Chem. 257, 5274–5282.

    Google Scholar 

  34. SEALE, R.L., ANNUZIATO, A.T., and SMITH, R.D. (1983). High mobility group proteins: abundance, turnover, and relationship to transcriptionally active chromatin. Biochemistry 22, 5008–5015.

    Article  PubMed  CAS  Google Scholar 

  35. GAREL, A. and AXEL, R. (1976). Selective digestion of transcriptionally active ovalbumin genes from oviduct nuclei. Proc. Nati. Acad. Sci. 73, 3960–3971.

    Google Scholar 

  36. SENEAR, A. W. and PALMITER, R. D. (1981). Multiple structural features are responsible for the nuclease sensitivity of the active ovalbumin gene. J. Biol. Chem. 256, 1191–1198.

    Google Scholar 

  37. REEVES, R. and CHANG, D. (1983). Investigations of the possible functions for glycosylation in the high mobility group proteins. J. Biol. Chem. 258, 679–687.

    Google Scholar 

  38. MATHEW, C.G.P., GOODWIN, G.H., IGO-KEMENES, T., and JOHNS, E.W. (1981). The protein composition of rat satellite chromatin. FEBS Lett. 125, 25–29.

    CAS  Google Scholar 

  39. ZHANG, X.Y. and HORZ, W. (1982). Analysis of highly purified satellite DNA containing chromatin from mouse. Nucleic Acids Res. 10, 1481–1494.

    Article  PubMed  CAS  Google Scholar 

  40. REUDELHUBER, T. L., BALL, D. J., DAVIS, A. H., and GERRARD, W.T. (1982). Transferring DNA from electrophoretically resolved nucleosomes to DBM-cellulose: properties of nucleosomes along mouse satellite DNA. Nucleic Acids Res. 10, 1311–1325.

    Article  PubMed  CAS  Google Scholar 

  41. STRAUSS, F. and VARSHAVSKY, A. (1984). A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome. Cell 37, 889 901.

    Google Scholar 

  42. WEISBROD, S. (1982). Properties of active nucleosomes as revealed by HMG-14 and 17 chromatography. Nucleic Acids Res. 10, 2017–2042.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1985 Plenum Press, New York

About this chapter

Cite this chapter

Goodwin, G.H., Nicolas, R.H., Wright, C.A., Zavou, S. (1985). The Structures and Functions of the Low Molecular Weight HMG Proteins. In: Reeck, G.R., Goodwin, G.H., Puigdomènech, P. (eds) Chromosomal Proteins and Gene Expression. NATO ASI Series, vol 101. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7615-6_15

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-7615-6_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-7617-0

  • Online ISBN: 978-1-4684-7615-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics