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.
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
WEINTRAUB, H. and GROUDINE, M. (1976). Chromosomal subunits in active genes have an altered conformation. Science 193, 848–858.
la. JOHNS, E.W., ed. (1983). “The HMG Chromosomal Proteins.” Academic Press, New York.
WEISBROD, S., GROUDINE, M., and WEINTRAUB, H. (1980). Interaction of HMG14 and 17 with actively transcribed genes. Cell 19, 289–299.
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.
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.
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.
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.
WALKER, J.M. (1982). Primary structures. In: “The HMG Chromosomal Proteins,” (E.W. Johns, ed.) pp.-b9–87. Academic Press, New York.
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.
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.
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.
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.
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.
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.
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.
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.
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.
COOPER, E. and SPAULDING, S.W. (1983). HMG-14/17-like proteins in calf thyroid. Biochem. J. 215, 643–649.
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.
REECK, G.R. and TELLER, D.C. (1985) proteins: purification, properties quence comparisons. In: “Progress Research,” Vol. II ( I Bekhor, ed.) Boca Raton, Florida.
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.
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.
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.
ALLFREY, V.G. (1982). Postsynthetic modifications. In: “The HMG Chromosomal Proteins, ( E.W. Johns, ed.) pp. 1148. Academic Press, New York and London.
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.
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.
RING, D. and COLE, R. D. (1979). Chemical cross-linking of H1 histone to the nucleosomal histone. J. Biol. Chem. 254, 11688–11695.
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.
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.
LEVY, W.B. and DIXON, G.H. (1978). Partial purification of transcriptionally active nucleosomes from trout testis cells. Nucleic Acids Res. 5, 4155–4167.
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.
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.
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.
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.
GAREL, A. and AXEL, R. (1976). Selective digestion of transcriptionally active ovalbumin genes from oviduct nuclei. Proc. Nati. Acad. Sci. 73, 3960–3971.
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.
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.
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.
ZHANG, X.Y. and HORZ, W. (1982). Analysis of highly purified satellite DNA containing chromatin from mouse. Nucleic Acids Res. 10, 1481–1494.
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.
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.
WEISBROD, S. (1982). Properties of active nucleosomes as revealed by HMG-14 and 17 chromatography. Nucleic Acids Res. 10, 2017–2042.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights 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