Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

Nature

Volumn 392, Issue 6671, 1998, Pages 42-48

  Chen, Lin ^a   Glovert, J N Mark ^a   Hogan, Patrick G ^b   Rao, Anjana ^b   Harrison, Stephen C ^a  

^a HARVARD UNIVERSITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; INTERLEUKIN 2; LYMPHOCYTE ANTIGEN RECEPTOR; NUCLEAR FACTOR; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR AP 1;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA CONFORMATION; HUMAN; IMMUNE RESPONSE; NONHUMAN; ONCOGENE C FOS; ONCOGENE C JUN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; T LYMPHOCYTE; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DNA; DNA-BINDING PROTEINS; GENE EXPRESSION REGULATION; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NFATC TRANSCRIPTION FACTORS; NUCLEAR PROTEINS; PROTEIN CONFORMATION; PROTO-ONCOGENE PROTEINS C-FOS; PROTO-ONCOGENE PROTEINS C-JUN; RECOMBINANT PROTEINS; T-LYMPHOCYTES; TRANSCRIPTION FACTOR AP-1; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

EID: 0032485391     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/32100     Document Type: Article

References (50)

1. Weiss, A. & Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274 (1994).
2. Crabtree, G. R. & Clipstone, N. A. Signal transmission between the plum membrane and nucleus of T lymphocytes. Annu. Rev. Biochem. 63, 1045-1083 (1994).
3. Jain, J., Loh, C. & Rao, A. Transcriptional regulation of the IL-2 gene. Curr. Opin. Immunol. 7, 333-342 (1995).
4. Serfling, E., Avots, A. & Neumann, M. The architecture of the interleukin-2 promoter: a reflection of T lymphocyte activation. Biochim. Biophys. Acta 1263, 181-200 (1995).
5. Shaw, J. P. et al. Identification of a putative regulator of early T cell activation genes. Science 241, 202-205 (1988).
6. Rao, A., Luo, C. & Hogan, P. G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15, 707-747 (1997).
7. Schreiber, S. L. & Crabtree, G. R. The mechanism of action of cyclosporin A and FK506. Immunol. Today 13, 136-142 (1992).
8. McCaffrey, P. G. et al. Isolation of the cyclosporin-sensitive T cell transcription factor NFATp. Science 262, 750-754 (1993).
9. Northrop, J. P. et al. NF-AT components define a family of transcription factors targeted in T-cell activation. Nature 369, 497-502 (1994).
10. Masuda, E. S. et al. NFATx, a novel member of the nuclear factor of activated T cells family that is expressed predominantly in the thymus. Mol. Cell Biol. 15, 2697-2706 (1995).
11. Hoey, T., Sun, Y. L., Williamson, K. & Xu, X. Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins. Immunity 2, 461-472 (1995).
12. Jain, J., Burgeon, E., Badalian, T. M., Hogan, P. G. & Rao, A. A similar DNA-binding motif in NFAT family proteins and the Rel homology region. J. Biol. Chem. 270, 4138-4145 (1995).
13. Chytil, M. & Verdine, G. L. The Rel family of eukaryotic transcription factors. Curr. Opin. Struct. Biol. 6, 91-100 (1996).
14. Shaw, K. T. et al. Immunosppressive drugs prevent a rapid dephosphorylation of transcription factor NFAT1 in stimulated immune cells. Proc. Natl Acad. Sci. USA 92, 11205-11209 (1995).
15. Timmerman, L. A., Clipstone, N. A., Ho, S. N., Northrop, J. P. & Crabtree, G. R. Rapid shuttling of NF-AT in discrimination of Ca2+ signals and immunosuppression. Nature 383, 837-840 (1996).
16. Luo, C. et al. Interaction of calcineurin with a domain of the transcription factor NFAT1 that controls nuclear import. Proc. Natl Acad. Sci. USA 93, 8907-8912 (1996).
17. Shibasaki, F., Price, E. R., Milan, D. & McKeon, F. Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4. Nature 382, 370-373 (1996).
18. Beals, C. R., Clipstone, N. A., Ho, S. N. & Crabtree, G. R. Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction. Genes Dev. 11, 824-834 (1997).
19. Liu, J. et al. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815 (1991).
20. Jain, J., McCaffrey, P. G., Valge-Archer, V. E. & Rao, A. Nuclear factor of activated T cells contains Fos and Jun. Nature 356, 801-304 (1992).
21. Jain, J., Miner, Z. & Rao, A. Analysis of the preexisting and nuclear forms of nuclear factor of activated T cells. J. Immunol. 151, 837-848 (1993).
22. Cockerill, P. N. et al. Human granulocyte-macrophage colony-stimulating factor enhancer function is associated with cooperative interactions between AP-1 and NFATp/c. Mol. Cell. Biol. 15, 2071-2079 (1995).
23. Jain, J. et al. The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun. Nature 365, 352-355 (1993).
24. Muller, C. W., Key, F. A., Sodeoka, M., Verdine, G. L. & Harrison, S. C. Structure of the NF-κB p50 homodimer bound to DNA. Nature 373, 311-317 (1995).
25. Ghosh, G., van Duyne, G., Ghosh, S. & Sigler, P. B. Structure of NF-κB p50 homodimer bound to a κB site. Nature 373, 303-310 (1995).
26. Wolfe, S. A. et al. Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc. Nature 385, 172-176 (1997).
27. Chen, L. et al. Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp. Curr. Biol. 5, 882-889 (1995).
28. Bork, P., Holm, L. & Sander, C. The immunoglobulin fold. Structural classification, sequence pattens and common core. J. Mol. Biol. 242, 309-320 (1994).
29. Ellenberger, T. E., Brandl, C. J., Struhl, K. & Harrison, S. C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell 71, 1223-1237 (1992).
30. Konig, P. & Richmond, T. J. The X-ray structure of the GCN4-bZlP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol 233, 139-154 (1993).
31. Glover, J. N. & Harrison, S. C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373, 257-261 (1995).
32. Seeman, N. C., Rosenberg, I. M. & Rich, A. Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl Acad. Sci. USA 73, 804-808 (1976).
33. Pabo, C. O. & Sauer, R. T. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61, 1053-1095 (1992).
34. Chen, L. Functional and Structural Studies of DNA Binding Proteins. Thesis, Harvard Univ., (1994).
35. Sun, L. J., Peterson, B. R. & Verdine, G. L. Dual role of the nuclear factor of activated T cells insert region in DNA recognition and cooperative contacts to activator protein 1. Proc. Natl Acad. Sci. USA 94, 4919-4924 (1997).
36. Peterson, B. R., Sun, L. J. & Verdine, G. L. A critical arginine residue mediates cooperativity in the contact interface between transcription factors NFAT and AP-1. Proc. Natl Acad. Sci. USA 93, 13671-13676 (1996).
37. Yamamoto, K. R., Pearce, D., Thomas, J. & Miner, J. N. in Transcriptional Regulation (eds McKnight, S. L. & Yamamoto, K. R.) 1169-1192 (Cold Spring Harbor Laboratory Press, NY, 1992).
38. Johnson, A. in Transcriptional Regulation (eds McKnight, S. L. & Yamamoto, K. R.) 975-1006 (Cold Spring Harbor Laboratory Press, NY, 1992).
39. Tjian, R. & Maniatis, T. Transcriptional activation: a complex puzzle with few easy pieces. Cell 77, 5-8 (1994).
40. Thanos, D. & Maniatis, T. Virus induction of human IFN beta gene expression requires the assembly of an enhanceosome. Cell 83, 1091-1100 (1995).
41. Garrity, P. A., Chen, D., Rothenberg, E. V. & Wold, B. J. Interleukin-2 transcription is regulated in vivo at the level of coordinated binding of both constitutive and regulated factors. Mol. Cell. Biol. 14, 2159-2169 (1994).
42. Otwinowski, Z. in Proceedings of the CCP4 study weekend (eds Sawyer, L., Isaacs, N. & Burley, S.) 56-62 (SERC Daresbury Laboratory, Warrington, 1993).
43. Collaborative Computational Project Number 4. The CCP suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-776 (1994).
44. Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58 (1991).
45. Jones, T. A., Bergdoll, M. & Kjeldgaard, M. in Crystallographic Computing and Modeling Methods in Molecular Design (eds Bugg, C. & Ealick, S.) (Springer, New York, 1989).
46. Brunger, A. T. X-PLOR Version 3.0: A System for Crystallography and NMR (Yale Univ. Press, New Haven, CT, 1992).
47. Kleywegt, G. & Jones, T. A. in From First Map to Final Model (eds Bailey, S., Hubbard, R. & Walker, D.) (Daresbury Laboratory, Warrington, 1994).
48. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
49. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
50. Carson, M. Ribbons 2.0. J. Appl. Crystallogr. 24, 958-961 (1991).