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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
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).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/286854a0
This article is cited by
-
Global histone protein surface accessibility in yeast indicates a uniformly loosely packed genome with canonical nucleosomes
Epigenetics & Chromatin (2021)
-
3D ATAC-PALM: super-resolution imaging of the accessible genome
Nature Methods (2020)
-
Long-range single-molecule mapping of chromatin accessibility in eukaryotes
Nature Methods (2020)
-
Phase separation of YAP reorganizes genome topology for long-term YAP target gene expression
Nature Cell Biology (2019)
-
NicE-seq: high resolution open chromatin profiling
Genome Biology (2017)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.