Abstract
On the basis of their primary structure, the lysine-rich histones are a unified family of proteins. Each has an amino acid chain which falls into three distinct domains. Only the central domain (∼80 residues) is in a folded conformation. It is protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation. Without the flanking domains it is able to close two full turns of DNA in the nucleosome and can thus locate the H1 molecule.
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References
Cole, R. D. in The Molecular Biology of the Mammalian Genetic Apparatus (ed. Ts'O, P.) 93 (Elsevier, Amsterdam, 1977).
Macleod, A. R., Wrong, N. C. & Dixon, G. H. Eur. J. Biochem. 78, 281–291 (1977).
Yaguchi, M., Roy, C. & Seligy, V. L. Biochem. biophys. Res. Commun. 90, 1400–1406 (1979).
Briand, G. et al. FEBS Lett. 112, 147–151 (1980).
Strickland, W. N. et al. Eur. J. Biochem. 104, 567–578 (1980).
Smith, B. J., Walker, J. M. & Johns, E. W. FEBS Lett. 112, 42–44 (1980).
Schaffner, W. et al. Cell 12, 655–671 (1978).
Bradbury, E. M. et al. Eur. J. Biochem. 52, 605–613 (1975).
Hartman, P. G., Chapman, G. E., Moss, T. & Bradbury, E. M. Eur. J. Biochem. 77, 45–51 (1977).
Aviles, F. J., Chapman, G. E., Kneale, G. G., Crane-Robinson, C. & Bradbury, E. M. Eur. J. Biochem. 88, 363–371 (1978).
Puigdomenech, P., Palau, J. & Crane-Robinson, C. Eur. J. Biochem. 104, 263–270 (1980).
Yaguchi, M., Roy, C., Dove, M. & Seligy, V. Biochem. biophys. Res. Commun. 76, 100–106 (1977).
Littau, V. C., Burdick, C. J., Allfrey, V. G. & Mirsky, A. E. Proc. natn. Acad. Sci. U.S.A. 54, 1204–1212 (1965).
Bradbury, E. M., Carpenter, B. G. & Rattle, H. W. E. Nature 241, 123–126 (1973).
Billett, M. A. & Barry, J. M. Eur. J. Biochem. 49, 477–484 (1974).
Noll, M. & Kornberg, R. D. J. molec. Biol. 109, 393–404 (1977).
Thoma, F., Koller, Th. & Klug, A. J. Cell Biol. 83, 403–426 (1979).
Allan, J., Staynov, D. Z. & Gould, H. Proc. natn. Acad. Sci. U.S.A. 77, 88–889 (1980).
Allan, J. et al. (in preparation).
Lutter, L. C. Nucleic Acids Res. 6, 41–56 (1979).
Tatchell, K. & Van Holde, K. E. Proc. natn. Acad. Sci. U.S.A. 75, 3583–3587 (1978).
Todd, R. D. & Garrard, W. T. J. biol. Chem. 254, 3074–3083 (1979).
Varshavsky, A. J., Bakayev, V. V. & Georgiev, G. P. Nucleic Acids Res. 3, 477–492 (1976).
Nelson, P. P., Albright, S. C., Wiseman, J. M. & Garrard, W. T. J. biol. Chem. 254, 11751–11760 (1979).
Simpson, R. T. Biochemistry 17, 5524–5531 (1978).
Bradbury, E. M., Chapman, G. E., Danby, S. E., Hartman, P. G. & Riches, P. L. Eur J. Biochem. 57, 521–528 (1975).
Chapman, G. E., Hartman, P. G., Cary, P. D., Bradbury, E. M. & Lee, D. R. Eur. J. Biochem. 86, 35–44 (1978).
Finch, J. T. et al. Nature 269, 29–36 (1977).
Singer, D. S. & Singer, M. Nucleic Acid Res. 3, 2531–2547 (1976).
Belyavsky, A. V., Bavykin, S. G., Goguadze, E. G. & Mirzabekov, A. D. J. molec. Biol. 139, 519–536 (1980).
Hayashi, K., Hofstaetler, T. & Yakuwa, N. Biochemistry 17, 1880–1883 (1978).
Olins, A. L., Carlson, R. D., Wright, E. B. & Olins, D. E. Nucleic Acids Res. 3, 3271–3291 (1976).
Weintraub, H. Nucleic Acids Res. 5, 1179–1188 (1978).
Goodwin, G. H., Nicholas, R. H. & Johns, E. W. Biochem. J. 167, 485–488 (1977).
Giancotti, V., Quadrifoglio, F., Cowgill, R. W. & Crane-Robinson, C. Biochim. biophys. Acta 624, 60–65 (1980).
Chapman, G. E., Hartman, P. G. & Bradbury, E. M. Eur. J. Biochem. 61, 69–75 (1976).
Goodwin, G. H., Walker, J. M. & Johns, E. W. Biochim. biophys. Acta 519, 233–242 (1978).
Panyim, S. & Chalkley, R. Archs Biochem. Biophys. 130, 337–346 (1969).
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Allan, J., Hartman, P., Crane-Robinson, C. et al. The structure of histone H1 and its location in chromatin. Nature 288, 675–679 (1980). https://doi.org/10.1038/288675a0
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DOI: https://doi.org/10.1038/288675a0
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