The Ig fold of the core binding factor α Runt domain is a member of a family of structurally and functionally related Ig-fold DNA-binding domains

Structure

Volumn 7, Issue 10, 1999, Pages 1247-1256

  Berardi, Marcelo J ^a   Sun, Chaohong ^a   Zehr, Michael ^a   Abildgaard, Frits ^b   Peng, Jeff ^c   Speck, Nancy A ^d   Bushweller, John H ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c VERTEX PHARMACEUTICALS   (United States)

^d DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

CBF; Core binding factor; Hematopoiesis; Leukemia; Transcription

Indexed keywords

DNA BINDING PROTEIN; IMMUNOGLOBULIN;

ARTICLE; BINDING AFFINITY; IMMUNOGLOBULIN STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0033569711     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)80058-1     Document Type: Article

References (32)

1. 1. Ogawa, E., et al., & Shigesada, K. (1993). Molecular cloning and characterization of PEBP2β, the heterodimeric partner of a novel Drosophila Runt-related DNA binding protein PEBP2α Virology 194, 314-331.
2. 2. Ogawa, E., et al., & Ito, Y. (1993). PEBP2/PEA2 represents a new family of transcription factor homologous to the products of the Drosophila runt and the human AML1 gene. Proc. Natl Acad. Sci. USA 90, 6859-6863.
3. 3. Kagoshima, H., et al., & Gergen, J.P. (1993). The Runt-domain identifies a new family of heteromeric DNA-binding transcriptional regulatory proteins. Trends Genet. 9, 338-341.
4. 4. Wang, S., Wang, Q., Crute, B.E., Melnikova, I.N., Keller, S.R. & Speck, N.A. (1993). Cloning and characterization of subunits of the T-cell receptor and murine leukemia virus enhancer core-binding factor. Mol. Cell. Biol. 13, 3324-3339.
5. 5. Meyers, S., Downing, J.R. & Hiebert, S.W. (1993). Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: the Runt homology domain is required for DNA binding and protein-protein interactions. Mol. Cell. Biol. 13, 6336-6345.
6. 6. Komori, T., et al., & Kishimoto, T. (1997). Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts. Cell 89, 755-764.
7. 7. Wang, Q., Stacy, T., Binder, M., Marin-Padilla, M., Sharpe, A.H. & Speck, N.A. (1996). Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the central nervous system and blocks definitive hematopoiesis. Proc. Natl Acad. Sci. USA 93, 3444-3449.
8. 8. Wang, Q., et al., & Speck, N.A. (1996). The CBFβ subunit is essential for CBFα2 (AML1) function in vivo. Cell 87, 697-708.
9. 9. Meyers, S. & Hiebert, S.W. (1995). Indirect and direct disruption of transcriptional regulation in cancer, E2F, and AML-1. Crit. Rev. Eukaryot. Gene Expr. 5, 365-383.
10. 10. Levanon, D., Eisenstein, M. & Groner, Y. (1998) Site-directed mutagenesis supports a three-dimensional model of the Runt domain. J. Mol. Biol. 277, 509-512.
11. 11. Huang, X., Peng, J.W., Speck, N.A. & Bushweller, J.H. (1999). Core binding factor β revealed, solution structure and map of the CBFα binding site. Nat. Struct. Biol. 6, 624-627.
12. 12. Bae, S.-C., et al., & Ito, Y. (1994). PEBP2aB/Mouse AML1 consists of multiple isoforms that possess differential transactivation potentials. Mol. Cell. Biol. 14, 3242-3252.
13. 13. Crute, B.E., Lewis, A.F., Wu, Z., Bushweller, J.H. & Speck, N.A. (1996). Biochemical and biophysical properties of the CBFα2 (AML1) DNA-binding domain. J. Biol. Chem. 271, 26251-26260.
14. 14. Thornell, A., Hallberg, B. & Grundstrom, T. (1991). Binding of SL3-3 enhancer factor 1 transcriptional activators to viral and chromosomal enhancer sequences. J. Virol. 65, 42-50.
15. 15. Wang, S. & Speck, N.A. (1992). Purification of core-binding factor, a protein that binds the conserved core site in murine leukemia virus enhancers. Mol. Cell. Biol. 12, 89-102.
16. 15N-amino acids. J. Biomol. NMR 8, 184-192.
17. 17. Rosen, M.K., Gardner, K.H., Willis, R.C., Parris, W.E., Pawson, T. & Kay L.E. (1996). Selective methyl group protonation of perdeuterated proteins. J. Mol. Biol. 263, 627-636.
18. 18. Gardner, K.H., Rosen, M.K. & Kay, L.E. (1997). Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry 36, 1389-1401.
19. 1H,-δ1 methyl) Isoleucine into proteins for multidimensional NMR studies. J. Am. Chem. Soc. 119, 7599-7600.
20. 13C magnetization. J. Magn. Reson. 101, 114-119.
21. 21. Cornilescu, G., Delaglio, F. & Bax, A. (1999). Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR, 13, 289-302.
22. 22. Bork, P., Holm, L. & Sander, C. (1994). The immunoglobulin fold structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320.
23. 23. Holm, L. & Sander, C. (1997). Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res. 25, 231-234.
24. 24. Chen, F.E., Huang D.B., Chen, Y.Q. & Ghosh, G. (1998). Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391, 410-413.
25. 25. Zhou, P., Sun, L.J., Dotsch, V., Wagner, G. & Verdine, G.L. (1998). Solution structure of the core NFATC1/DNA complex. Cell 92, 687-696.
26. 26. Cho, Y., Gorina, S., Jeffrey, P.D. & Pavletich, N.P. (1994). Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265, 346-355.
27. 27. Chen, X., Vinkemeier, U., Zhao, Y., Jeruzalmi, D., Darnell, J.E., Jr. & Kuriyan, J. (1998). Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 93, 827-839.
28. 28. Muller, C.W. & Herrmann, B.G. (1997). Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor. Nature 389, 884-888.
29. 29. Akamatsu, Y., Tsukumo, S., Kagoshima, H., Tsurushita, N. & Shigesada, K. (1996). A simple screening for mutant DNA binding proteins: application to murine transcription factor PEBP2a subunit, a founding member of the Runt domain protein family. Gene 185, 111-117.
30. 30. Golling, G., Li, L.-H., Pepling, M., Stebbins, M. & Gergen, J.P. (1996). Drosophila homologues of proto-oncogene product PEBP2/CBFb regulate the DNA-binding properties of Runt. Mol. Cell. Biol. 16, 932-942.
31. 31. Kanno, T., Kanno, Y., Chen, L.-F., Ogawa, E, Kim, W.Y. & Ito, Y. (1998). Intrinsic transcriptional activation-inhibition domains of the polyomavirus enhancer binding protein 2/core binding factor α subunit revealed in the presence of the β subunit. Mol. Cell. Biol. 18, 2444-2454.
32. 32. Chen, L., Glover, J.N.M., Hogan, P.G., Rao, A. & Harrison, S.C. (1998). Structure of the DNA-binding domains from NFAT, Fos, and Jun bound specifically to DNA. Nature 392, 42-48.