Nature Publishing Group, publisher of Nature, and other science journals and reference works
Nature
my account e-alerts subscribe register
   
Saturday 11 July 2009
Journal Home
Current Issue
AOP
Archive
THIS ARTICLE
Download PDF
References
Export citation
Export references
Send to a friend
More articles like this
Table of Contents
< Previous | Next >

Article
Nature 353, 822 - 827 (31 October 1991); doi:10.1038/353822a0

Stress-induced oligomerization and chromosomal relocalization of heat-shock factor

J. Timothy Westwood, Joachim Clos & Carl Wu

Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bg 37, Rm 4C-09, Bethesda, Maryland 20892, USA

The induction of heat-shock transcription factor (HSF) binding to DNA is accomplished by a heat-induced oligomerization. The transition to the induced state is accompanied by a chromosomal redistribution of HSF to the heat-shock puff sites. Over 150 additional chromosomal sites also accumulate HSF, including developmental loci that are repressed during heat shock. These findings suggest an unforeseen role for HSF as a represser of normal gene activity during heat stress.

------------------

References
1. Morimoto, R. I., Tissieres, A. & Georgopoulos, C. (eds) Stress Proteins in Biology and Medicine (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1990).
2. Ritossa, F. Experientia 18, 571−573 (1962).
3. Pelham, H. R. B. in Stress Proteins in Biology and Medicine (eds Morimoto, R. I., Tissieres, A. & Georgopoulos, C.) 287−300 (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1990).
4. Ellis, R. J. & van der Vies, S. M. A. Rev. Biochem. 60, 321−347 (1991).
5. Pelham, H. R. B. Cell 30, 517−528 (1982).
6. Amin, J., Ananthan, J. & Voellmy, R. Molec. cell. Biol. 8, 3761−3769 (1988).
7. Xiao, H. & Lis, J. T. Science 239, 1139−1142 (1988).
8. Wu, C. in Stress Proteins in Biology and Medicine (eds Morimoto, R. I., Tissieres, A. & Georgopoulos, C.) 429−442 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1990).
9. Sorger, P. Cell 65, 363−366 (1991).
10. Sorger, P. K. & Pelham, H. R. B. Cell 54, 855−864 (1988).
11. Wiederrecht, G., Seto, D. & Parker, C. S. Cell 54, 841−843 (1988).
12. Clos, J. et al. Cell 63, 1085−1097 (1990).
13. Scharf, K.-D., Rose, S., Zott, W., Schoff, F. & Nover, L. EMBO J. 9, 4495−4501 (1990).
14. Jakobsen, B. K. & Pelham, H. R. B. EMBO J. 10, 369−375 (1991).
15. Rabindran, S. R., Giorgi, G., Clos, J. & Wu, C. Proc. natn. Acad. Sci. U.S.A. 88, 6906−6910 (1991).
16. Schuetz, T. J., Gallo, G., Sheldon, L., Tempst, P. & Kingston, R. E. Proc. natn. Acad. Sci. U.S.A. 88, 7911−7915 (1991).
17. Sarge, K. D., Zimarino, V., Holm, K., Wu, C. & Morimoto, R. I. Genes Dev. (in the press).
18. Larson, J. S., Schuetz, T. J. & Kingston, R. E. Nature 335, 372−375 (1988).
19. Mosser, D. D., Kotzbauer, P. T., Sarge, K. D. & Morimoto, R. Proc. natn. Acad. Sci. U.S.A. 87, 3748−3752 (1990).
20. Becker, J., Mezger, V., Courgeon, A.-M. & Best-Belpomme, M. Eur. J. Biochem. 189, 553−558 (1990).
21. Zimarino, V., Wilson, S. & Wu, C. Science 249, 546−549 (1990).
22. Perisic, O., Xiao, H. & Lis, J. T. Cell 59, 797−806 (1989).
23. Sorger, P. K. & Nelson, H. C. M. Cell 59, 807−813 (1989).
24. Andersson, L. O., Borg, H. & Mikaelsson, M. FEBS Lett. 20, 199−201 (1972).
25. Wu, C. et al. Science 238, 1247−1253 (1987).
26. King, W. J. & Greene, G. L. Nature 307, 745−747 (1984).
27. Welshons, W. V., Lieberman, M. E. & Gorski, J. Nature 307, 747−749 (1984).
28. Silver, L. M. & Elgin, S. C. R. Proc. natn. Acad. Sci. U.S.A. 73, 423−427 (1976).
29. Jamrich, M., Greenleaf, A. L. & Bautz, E. K. F. Proc. natn. Acad. Sci. U.S.A. 74, 2079−2083 (1977).
30. Zink, B. & Paro, R. Nature 337, 468−471 (1989).
31. Ashburner, M. Chromosoma 31, 356−376 (1970).
32. Lis, J., Ish-Horowicz, D. & Pinchin, S. M. Nucleic Acids Res. 9, 5297−5310 (1981).
33. Mason, P. J., Torok, I., Kiss, I., Karch, F. & Udvardy, A. J. molec. Biol. 156, 21−35 (1982).
34. Lakhotia, S. C. J. Genet. 66, 139−157 (1987).
35. Bonner, J. J. & Pardue, M. L. Cell 8, 43−50 (1976).
36. Hovemann, B., Walldorf, U. & Ryseck, R.-P. Molec. Gen. Genet. 204, 334−340 (1986).
37. Lis, J. T., Neckameyer, W., Dubensky, R. & Costlow, N. Gene 15, 67−80 (1981).
38. Spradling, A., Pardue, M. L. & Penman, S. J. molec. Biol. 109, 559−587 (1977).
39. Bonner, J. J. & Kerby, R. L. Chromosoma 85, 93−108 (1982).
40. Pardue, M. L., Kedes, L. H., Weinberg, E. & Birnstiel, M. L. Chromosoma 63, 135−152 (1977).
41. Palter, K. B., Watanabe, M., Stinson, L., Mahowals, A. P. & Craig, E. A. Molec. cell. Biol. 6, 1187−1203 (1986).
42. Lindquist, S. & Craig, E. A. A. Rev. Genet. 22, 631−677 (1988).
43. Perkins, L. A. et al. Molec. cell. Biol. 10, 3232−3238 (1990).
44. Ashburner, M. in Results and Problems in Cell Differentiation Vol. 4 (eds Beermann, W. et al.) 101−151 (Springer, New York, 1972).
45. Burtis, K. C., Thummel, C. S., Jones, C. W., Karim, F. D. & Hogness, D. S. Cell 61, 85−99 (1990).
46. Urness, L. D. & Thummel, C. S. Cell 63, 47−61 (1990).
47. Seagraves, W. A. & Hogness, D. S. Genes Dev. 4, 204−219 (1990).
48. Thummel, C. S. Bioessays 12, 561−568 (1990).
49. Wu, C., Nature 309, 229−234 (1984).
50. Wu, C. Nature 311, 81−84 (1984).
51. Wu, C. Nature 317, 84−87 (1985).
52. Parker, C. S. & Topol, J. Cell 36, 357−369 (1984).
53. Wiederrecht, G., Shuey, D. J., Kibbe, W. & Parker, C. S. Cell 48, 507−515 (1987).
54. Dignam, A. D., Martin, P. L., Shastry, B. S. & Roeder, R. G. Meth. Enzym. 191, 582−598 (1983).
55. Bridges, C. B. J. Hered. 26, 60−64 (1935).
56. Lefevre, G. in The Genetics and Biology of Drosophila Vol. 1a (eds Ashburner, M. & Novitski, E.) 31−66 (Academic, New York, 1976).


© 1991 Nature Publishing Group
Privacy Policy