Abstract
Many specific sites in Drosophila chromatin are hypersensitive to DNase I. The positions of such sites were mapped along the regions of the genome coding for two heat shock proteins. Such sites lie at the 5′ ends of heat shock genes and may function as elements for recognition by molecules which regulate gene activity.
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References
Felsenfeld, G. Nature 271, 115–122 (1978).
Wu, C., Bingham, P. M., Livak, K. J., Holmgren, R. & Elgin, S. C. R. Cell 16, 797–806 (1979).
Southern, E. M. J. molec. Biol. 98, 503–517 (1975).
Schneider, I. J. Embryol. exp. Morph. 27, 353–365 (1972).
Ashburner, M. & Bonner, J. J. Cell 17, 214–254 (1979).
Ritossa, F. Experientia 18, 571–573 (1962).
Ashburner, M. Chromosoma 31, 356–376 (1970).
Tissieres, A., Mitchell, H. K. & Tracy, U. M. J. molec. Biol. 84, 389–398 (1974).
McKenzie, S. L., Henikoff, S. & Meselson, M. Proc. natn. Acad. Sci. U.S.A. 72, 1117–1121 (1975).
Spradling, A., Penman, S. & Pardue, M. L. Cell 4, 395–404 (1975).
Lewis, M., Helmsing, P. J. & Ashburner, M. Proc. natn. Acad. Sci. U.S.A. 72, 3604–3608 (1975).
Spradling, A., Pardue, M. L. & Penman, S. J. molec. Biol. 109, 559–587 (1977).
McKenzie, S. L. & Meselson, M. J. molec. Biol. 117, 279–283 (1977).
Mirault, M. E., Goldschmidt-Clermont, M., Moran, L., Arrigo, A. P. & Tissieres, A. Cold Spring Harb. Symp. quant. Biol. 42, 819–829 (1978).
Henikoff, S. & Meselson, M. Cell 12, 441–451 (1977).
Ish-Horowicz, D., Holden, J. J. & Gehring, W. J. Cell 12, 643–652 (1977).
Livak, K. J., Freund, R., Schweber, M., Wensink, P. C. & Meselson, M. Proc. natn. Acad. Sci. U.S.A. 75, 5613–5617 (1978).
Schedl, P. et al. Cell 14, 921–929 (1978).
Craig, E. A., McCarthy, B. J. & Wadsworth, S. C. Cell 16, 575–588 (1979).
Moran, L. et al. Cell 17, 1–8 (1979).
Artavanis-Tsakonas, S., Schedl, P., Mirault, M. E., Moran, L. & Lis, J. Cell 17, 9–18 (1979).
Mirault, M. E., Goldschmidt-Clermont, M., Artavanis-Tsakonas, S. & Schedl, P. Proc. natn. Acad. Sci. U.S.A. 76, 5254–5258 (1979).
Ish-Horowicz, D., Pinchin, S. M., Schedl, P., Artavanis-Tsakonas, S. & Mirault, M. E. Cell 18, 1351–1358 (1979).
Holmgren, R., Livak, K., Morimoto, R., Freund, R. & Meselson, M. Cell 18, 1359–1370 (1979).
Goldschmidt-Clermont, M. Nucleic Acids Res. 8, 235–251 (1980).
Bernardi, A., Gaillard, C. & Bernardi, G. Eur. J. Biochem. 52, 451–457 (1975).
Lis, J. T., Prestidge, L. & Hogness, D. S. Cell 14, 901–919 (1978).
Wu, C., Wong, Y. C. & Elgin, S. C. R. Cell 16, 807–814 (1979).
Wensink, P. C., Finnegan, D. J., Donelson, J. E. & Hogness, D. S. Cell 3, 315–325 (1974).
Wu, C. thesis, Harvard Univ. (1979).
Anfinsen, C. B., Cuatrecasas, P. & Taniuchi, H. in The Enzymes Vol. IV, 3rd edn (ed. Boyer, P. D.) 177–199 (Academic, New York, 1971).
Ponder, B. A. & Crawford, C. V. Cell 11, 35–49 (1977).
Musich, P. R., Maio, J. J. & Brown, F. L. J. molec. Biol. 117, 657–677 (1977).
Chao, M. V., Gralla, J. & Martinson, H. G. Biochemistry 8, 1068–1074 (1979).
Wittig, B. & Wittig, S. Cell 18, 1173–1183 (1979).
Fittler, F. & Zachau, H. G. Nucleic Acids Res. 7, 1–13 (1979).
Scott, W. A. & Wigmore, D. J. Cell 15, 1511–1518 (1978).
Varshavsky, A. J., Sundin, O. & Bohn, M. Cell 16, 453–466 (1979).
Waldeck, W., Fohring, B., Chowdhury, K., Gruss, P. & Sauer, G. Proc. natn. Acad. Sci. U.S.A. 75, 5964–5968 (1978).
Kuo, M. T., Mandel, J. L. & Chambon, P. Nucleic Acids Res. 7, 2105–2113 (1979).
Hayward, G. S. & Smith, M. G. J. molec. Biol. 63, 383–395 (1972).
Wahl, G. M., Stern, M. & Stark, G. R. Proc. natn. Acad. Sci. U.S.A. 76, 3683–3687 (1979).
Denhardt, D. Biochem. biophys. Res. Commun. 23, 641–646 (1966).
Sutcliffe, J. G. Nucleic Acids Res. 5, 2721–2728 (1978).
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Wu, C. The 5′ ends of Drosophila heat shock genes in chromatin are hypersensitive to DNase I. Nature 286, 854–860 (1980). https://doi.org/10.1038/286854a0
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DOI: https://doi.org/10.1038/286854a0
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