Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-κB

Abstract

The c-Rel protein is able to associate in vitro and in vivo with the TATA-binding protein (TBP) of the TFIID complex. Coexpression of TBP with c-Rel augments transactivation from the κB site in Drosophila Schneider cells. DNA-binding mutants of TBP not only fail to cooperate, but they repress transactivation by c-Rel. There may be a direct communication between κB enhancer binding proteins and basal transcription factors which leads to enhanced transcription.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Suzuki, Y. et al. Proc. natn. Acad. Sci. U.S.A. 83, 9522–9526 (1986).

  2. 2

    Gorski, K., Carneiro, M. & Schibler, U. Cell 47, 767–776 (1986).

  3. 3

    Heintz, N. & Roeder, R. G. Proc. natn. Acad. Sci. U.S.A. 81, 2713–2717 (1984).

  4. 4

    Topol, J., Ruden, D. M. & Parker, C. S. Cell 42, 527–537 (1985).

  5. 5

    Gilmore, T. D. Cancer Surv. 15, 69–87 (1992).

  6. 6

    Kao, K. R. & Hopwood, N. D. Proc. natn. Acad. Sci. U.S.A. 88, 2697–2701 (1991).

  7. 7

    Ryseck, R.-P. et al. Molec. Cell. Biol. 12, 674–684 (1992).

  8. 8

    Kieran, M. et al. Cell 62, 1007–1018 (1990).

  9. 9

    Ghosh, S. et al. Cell 62, 1019–1029 (1990).

  10. 10

    Nolan, G. P., Ghosh, S., Lion, H.-C., Tempst, P. & Baltimore, D. Cell 64, 961–969 (1991).

  11. 11

    Ruben, S. M. et al. Science 251, 1490–1493 (1991).

  12. 12

    Schmid, R. M., Perkins, N. D., Duckett, C. S., Andrews, P. C. & Nabel, G. J. Nature 352, 733–736 (1991).

  13. 13

    Bours, V. et al. Molec. cell. Biol. 12, 685–695 (1992).

  14. 14

    Steward, R. Science 238, 692–694 (1987).

  15. 15

    Bull, P., Morley, K. L., Hoekstra, M. F., Hunter, T. & Verma, I. M. Molec. cell. Biol. 10, 5473–5485 (1990).

  16. 16

    Schmitz, M. L. & Baeuerle, P. A. EMBO J. 10, 3805–3817 (1991).

  17. 17

    Pan, D., Huang, J.-D. & Courey, A. J. Genes Dev. 5, 1892–1901 (1991).

  18. 18

    Roeder, R. G. Trends biochem. Sci. 16, 402–408 (1991).

  19. 19

    Hoffman, A. et al. Nature 346, 387–390 (1990).

  20. 20

    Peterson, M. G., Tanese, N., Pugh, B. F. & Tjian, R. Science 248, 1625–1630 (1990).

  21. 21

    Tanese, N., Pugh, B. F. & Tjian, R. Genes Dev. 5, 2212–2224 (1991).

  22. 22

    Dynlacht, B. D., Hoey, T. & Gjian, R. Cell 55, 563–576 (1991).

  23. 23

    Zhou, Q., Lieberman, P. M., Boyer, T. G. & Berk, A. J. Genes Dev. 6, 1964–1974 (1992).

  24. 24

    Maldonada, E., Ha, I., Cortes, P., Weiss, L. & Reinberg, D. Molec. cell. Biol. 10, 6335–6347 (1990).

  25. 25

    Cortes, P., Flores, O. & Reinberg, D. Molec. cell. Biol. 12, 413–421 (1992).

  26. 26

    Coulombe, B. et al. Gene Exp. 2, 99–110 (1992).

  27. 27

    Meisterernst, M. & Roeder, R. G. Cell 6, 557–567 (1991).

  28. 28

    Inostroza, J. A., Mermelstein, F. H., Ha, I., Lane, W. S. & Reinberg, D. Cell. 70, 477–489 (1992).

  29. 29

    Usheva, A. et al. Cell 69, 871–881 (1992).

  30. 30

    Stringer, K. F., Ingles, C. J. & Greenblatt, J. Nature 345, 783–786 (1990).

  31. 31

    Ingles, C. J., Shales, M., Cress, W. D., Triezenberg, S. J. & Greenblatt, J. Nature 351, 588–590 (1991).

  32. 32

    Lieberman, P. M. & Berk, A. J. Genes Dev. 5, 2441–2454 (1991).

  33. 33

    Lee, W. S., Kao, C., Bryant, G. O., Liu, X. & Berk, A. J. Cell 67, 365–376 (1991).

  34. 34

    Horikoshi, N. et al. Proc. natn. Acad. Sci. U.S.A. 88, 5124–5128 (1991).

  35. 35

    Horikoshi, M., Carey, M. F., Kakidani, H. & Roeder, R. G. Cell 54, 655–669 (1988).

  36. 36

    Zhu, H., Roy, A. L., Roeder, R. G. & Prywes, R. New Biologist 3, 455–464 (1991).

  37. 37

    Colgan, J. & Manley, J. L. Genes Dev. 6, 304–315 (1992).

  38. 38

    Inoue, J.-I. et al. Proc. natn. Acad. Sci. U.S.A. 89, 4333–4337 (1992).

  39. 39

    Yamamoto, T. et al. Proc. natn. Acad. Sci. U.S.A. 89, 2844–2848 (1992).

  40. 40

    Lee, D. K., Dejong, J., Hashimoto, S., Horikoshi, M. & Roeder, R. G. Molec. cell. Biol. 12, 5189–5196 (1992).

  41. 41

    Horikoshi, M. et al. Nature 341, 299–303 (1989).

  42. 42

    Greenblat, J. Nature 360, 16–17 (1992).

  43. 43

    Reddy, P. & Hahn, S. Cell 65, 349–357 (1991).

  44. 44

    Inoue, J.-I. et al. Proc. natn. Acad. Sci. U.S.A. 88, 3715–3719 (1991).

  45. 45

    Kumar, S., Rabson, A. & Gelinar, C. Molec. cell. Biol. 12, 3094–3106 (1992).

  46. 46

    Kelleher, R. J. et al. Genes Dev. 6, 296–303 (1992).

  47. 47

    Seto, E. et al. Proc. natn. Acad. Sci. U.S.A. 89, 12028–12032 (1992).

  48. 48

    Nikolov, D. B. et al. Nature 360, 40–46 (1992).

  49. 49

    Ip, Y. T., Kraut, R., Levine, M. & Rushlow, C. A. Cell 64, 439–446 (1991).

  50. 50

    Hahn, S., Buratowski, S., Sharp, P. A. & Guarente, L. Cell 58, 1173–1181 (1989).

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Further reading

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.