X-ray structures of Myc-Max and Mad-Max recognizing DNA: Molecular bases of regulation by proto-oncogenic transcription factors

Cell

Volumn 112, Issue 2, 2003, Pages 193-205

  Nair, Satish K ^a,c   Burley, Stephen K ^a,b  

^a ROCKEFELLER UNIVERSITY   (United States)

^b ELI LILLY AND COMPANY   (United States)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DNA; HELIX LOOP HELIX PROTEIN; LEUCINE ZIPPER PROTEIN; MAX PROTEIN; PROTEIN MAD1; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BURKITT LYMPHOMA; CANCER; CELL DIFFERENTIATION; CELL PROLIFERATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEREGULATION; DIMERIZATION; DNA BINDING; E BOX ELEMENT; GENE TARGETING; HUMAN; LUNG SMALL CELL CANCER; NEUROBLASTOMA; ONCOGENE MYC; PRIORITY JOURNAL;

HOMO;

EID: 0037462459     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01284-9     Document Type: Article

References (70)

1. Ayer D.E., Kretzner L., Eisenman R.N. Mad. a heterodimeric partner for max that antagonizes Myc transcriptional activity Cell. 72:1993;211-222.
2. Ayer D.E., Lawrence Q.A., Eisenman R.N. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell. 80:1995;767-776.
3. Baca M., Muir T.W., Schnölzer M., Kent S.B.H. Chemical ligation of cysteine-containing peptides. synthesis of a 22 kDA tethered dimer of HIV-1 protease J. Am. Chem. Soc. 117:1995;1881-1887.
4. Bao J., Zervos A.S. Isolation and characterization of Nmi, a novel partner of Myc proteins. Oncogene. 12:1996;2171-2176.
5. Benvenisty N., Ornitz D.M., Bennett G.L., Sahagan B.G., Kuo A., Cardiff R.D., Leder P. Brain tumours and lymphomas in transgenic mice that carry HTLV-I LTR/c-myc and Ig/tax genes. Oncogene. 7:1992;2399-2405.
6. Blackwood E., Eisenman R.N. Max. a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc Science. 251:1991;1211-1217.
7. Brownlie P., Ceska T., Lamers M., Romier C., Stier G., Teo H., Suck D. The crystal structure of an intact human Max-DNA complex. new insights into mechanisms of transcriptional control Structure. 5:1997;509-520.
8. Brünger A.T. X-PLOR. A system for X-ray crystallography and NMR:1992;Yale University Press, New Haven.
9. Brünger A., Adams P.D., Clore G.M., Gros P., Grosse-Kuntsleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., Read R.J. Crystallography and NMR system. a new software system for macromolecular structure determination Acta Crystallogr. D. 54:1998;905-921.
10. Carey M. The enhanceosome and transcriptional synergy. Cell. 92:1998;5-8.
11. Coller H.A., Grandori C., Tamayo P., Colbert T., Lander E.S., Eisenman R.N., Golub T.R. Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion. Proc. Natl. Acad. Sci. USA. 97:2000;3260-3265.
12. Cole M.D., McMahon S.B. The Myc oncoprotein. a critical evaluation of transactivation and target gene regulation Oncogene. 18:1999;2916-2924.
13. Dalla-Favera R., Bregni M., Erikson J., Patterson D., Gallo R.C., Croce C.M. Human c-myc onc gene is located on the region of chromosome 8 that is translocated in Burkitt lymphoma cells. Proc. Natl. Acad. Sci. USA. 79:1982;7824-7827.
14. Dang C.V., Dolde C., Gillison M.L., Kato G.J. Discrimination between related DNA sites by a single amino-acid residue of Myc-related basic-helix-loop-helix proteins. Proc. Natl. Acad. Sci. USA. 89:1992;599-602.
15. Dang C.V., McGuire M., Buckmire M., Lee W.M. Involvement of the 'leucine zipper' region in the oligomerization and transforming activity of human c-myc protein. Nature. 337:1989;664-666.
16. Dang C.V., Resar L.M., Emison E., Kim S., Li Q., Prescott J.E., Wonsey D., Zeller K. Function of the c-Myc oncogenic transcription factor. Exp. Cell Res. 253:1999;63-77.
17. Eilers M. Control of cell proliferation by Myc family genes. Mol. Cells. 9:1999;1-6.
18. Eilers M., Schirm S., Bishop J.M. The MYC protein activates transcription of the alpha-prothymosin gene. EMBO J. 10:1991;133-141.
19. Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices. crystal structure of the protein-DNA complex Cell. 71:1992;1223-1237.
20. Ferre-D'Amare A.R., Prendergast G.C., Ziff E.B., Burley S.K. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature. 363:1993;38-45.
21. Fisher D.E., Parent L.A., Sharp P.A. Myc/Max and other helix-loop-helix/leucine zipper proteins bend DNA toward the minor groove. Proc. Natl. Acad. Sci. USA. 89:1992;11779-11783.
22. Gaubatz S., Imhof A., Dosch R., Werner O., Mitchell P., Buettner R., Eilers M. Transcriptional activation by Myc is under negative control by the transcription factor AP-2. EMBO J. 14:1995;1508-1519.
23. Grandori C., Eisenman R.N. Myc target genes. Trends Biochem. Sci. 22:1997;177-181.
24. Grandori C., Mac J., Siebelt F., Ayer D.E., Eisenman R.N. Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo. EMBO J. 15:1996;4344-4357.
25. Hassig C.A., Fleischer T.C., Billin A.N., Schreiber S.L., Ayer D.E. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell. 89:1997;341-347.
26. Hill C.P., Osslund T.D., Eisenberg D. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. USA. 90:1993;5167-5171.
27. Hurlin P.J., Ayer D.E., Grandori C., Eisenman R.N. The Max transcription factor network. involvement of Mad in differentiation and an approach to identification of target genes Cold Spring Harb. Symp. Quant. Biol. 59:1994;109-116.
28. Janin J. Specific versus non-specific contacts in protein crystals. Nat. Struct. Biol. 4:1997;973-974.
29. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
30. Kohl N.E., Kanda N., Schreck R.R., Bruns G., Latt S.A., Gilbert F., Alt F.W. Transposition and amplification of oncogene-related sequences in human neuroblastomas. Cell. 35:1983;359-367.
31. Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24:1991;946-950.
32. Kretzner L., Blackwood E.M., Eisenman R.N. Transcriptional activities of the Myc and Max proteins in mammalian cells. Curr. Top. Microbiol. Immunol. 182:1992;435-443.
33. Laherty C.D., Yang W.M., Sun J.M., Davie J.R., Seto E., Eisenman R.N. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell. 89:1997;349-356.
34. Larsson L.G., Bahram F., Burkhardt H., Luscher B. Analysis of the DNA-binding activities of Myc/Max/Mad network complexes during induced differentiation of U-937 monoblasts and F9 teratocarcinoma cells. Oncogene. 15:1997;737-748.
35. Larsson L.G., Pettersson M., Oberg F., Nilsson K., Luscher B. Expression of mad, mxi1, max and c-myc during induced differentiation of hematopoietic cells. opposite regulation of Mad and c-Myc Oncogene. 9:1994;1247-1252.
36. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. Procheck. a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26:1993;283-291.
37. Liao D.J., Dickson R.B. c-Myc in breast cancer. Endocr. Relat. Cancer. 7:2000;143-164.
38. McArthur G.A., Laherty C.D., Queva C., Hurlin P.J., Loo L., James L., Grandori C., Gallant P., Shiio Y., Hokanson W.C.et al. The Mad protein family links transcriptional repression to cell differentiation. Cold Spring Harb. Symp. Quant. Biol. 63:1998;423-433.
39. McMahon S.B., Wood M.A., Cole M.D. The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol. Cell. Biol. 20:2000;556-562.
40. Merika M., Thanos D. Enhanceosomes. Curr. Opin. Genet. Dev. 11:2001;205-208.
41. Merritt E.A., Murphy M.E.P. Raster3D Version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. D. 50:1994;869-873.
42. Moore J.P., Hancock D.C., Littlewood T.D., Evan G.I. A sensitive and quantitative enzyme-linked immunosorbence assay for the c-Myc and n-myc oncoproteins. Oncogene Res. 2:1987;65-80.
43. Nau M.M., Brooks B.J., Battey J., Sausville E., Gazdar A.F., Kirsch I.R., McBride O.W., Bertness V., Hollis G.F., Minna J.D. L-Myc, a new Myc-related gene amplified and expressed in human small cell lung cancer. Nature. 318:1985;69-73.
44. Navaza J. AmoRe. an automated program for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
45. Nekludova L., Pabo C.O. Distinctive DNA conformations with enlarged major groove is found in Zn-finger-DNA and other protein-DNA complexes. Proc. Natl. Acad. Sci. USA. 91:1994;6948-6952.
46. Nesbit C.E., Tersak J.M., Prochownik E.V. MYC oncogenes and human neoplastic disease. Oncogene. 18:1999;3004-3016.
47. Nicholls A., Sharp K., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
48. O'Hagan R.C., Schreiber-Agus N., Chen K., David G., Engelman J.A., Schwab R., Alland L., Thomson C., Ronning D.R., Sacchettini J.C.et al. Gene-target recognition among members of the myc superfamily and implications for oncogenesis. Nat. Genet. 24:2000;113-119.
49. O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 254:1991;539-544.
50. Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Meth. Enzymol., J. Charles, W. Carter, and R.M. Sweet, eds., pp. 307-326.
51. Parraga A., Bellsolell L., Ferre-D'Amare A.R., Burley S.K. Co-crystal structure of sterol regulatory element binding protein 1a at 2.3Å resolution. Structure. 6:1998;661-672.
52. Peukert K., Staller P., Schneider A., Carmichael G., Hanel F., Eilers M. An alternative pathway for gene regulation by Myc. EMBO J. 16:1997;5672-5686.
53. Prendergast G.C., Lawe D., Ziff E.B. Association of Myn, the murine homolog of Max with c-Myc stiumulates methylation-sensitive DNA binding and Ras cotransformation. Cell. 65:1991;395-407.
54. Robinson R.C., Grey L.M., Staunton D., Vankelecom H., Vernallis A.B., Moreau J.F., Stuart D.I., Heath J.K., Jones E.Y. The crystal structure and biological function of leukemia inhibitory factor. implications for receptor binding Cell. 77:1994;1101-1116.
55. Rudolph C., Adam G., Simm A. Determination of copy number of c-Myc protein per cell by quantitative Western blotting. Anal. Biochem. 269:1999;66-71.
56. Sakamuro D., Prendergast G.C. New Myc-interacting proteins. a second Myc network emerges Oncogene. 18:1999;2942-2954.
57. Saleh A., Schieltz D., Ting N., McMahon S.B., Litchfield D.W., Yates J.R., Lees-Miller S.P., Cole M.D., Brandl C.J. Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes. J. Biol. Chem. 273:1998;26559-26565.
58. Schreiber-Agus N., Chin L., Chen K., Torres R., Rao G., Guida P., Skoultchi A.I., DePinho R.A. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell. 80:1995;777-786.
59. Schwab M., Varmus H.E., Bishop J.M., Grzeschik K.H., Naylor S.L., Sakaguchi A.Y., Brodeur G., Trent J. Chromosome localization in normal human cells and neuroblastomas of a gene related to c-Myc. Nature. 308:1984;288-291.
60. Sheiness D., Fanshier L., Bishop J.M. Identification of nucleotide sequences which may encode the oncogenic capacity of avian retrovirus MC29. J. Virol. 28:1978;600-610.
61. Shim H., Dolde C., Lewis B.C., Wu C.S., Dang G., Jungmann R.A., Dalla-Favera R., Dang C.V. c-Myc transactivation of LDH-A. implications for tumor metabolism and growth Proc. Natl. Acad. Sci. USA. 94:1997;6658-6663.
62. Somers W., Stahl M., Seehra J.S. 1.9 Å crystal structure of interleukin 6. implications for a novel mode of receptor dimerization and signaling EMBO J. 16:1997;989-997.
63. Sui H., Han B.G., Lee J.K., Walian P., Jap B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature. 414:2001;872-878.
64. Taub R., Kirsch I., Morton C., Lenoir G., Swan D., Tronick S., Aaronson S., Leder P. Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells. Proc. Natl. Acad. Sci. USA. 79:1982;7837-7841.
65. Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., Shiina M., Kimura K., Takata S., Fujikawa A., Morii H.et al. Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter. Cell. 108:2002;57-70.
66. Wang Q., Zhang H., Kajino K., Greene M.I. BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells. Oncogene. 17:1998;1939-1948.
67. Watson D.K., Psallidopoulos M.C., Samuel K.P., Dalla-Favera R., Papas T.S. Nucleotide sequence analysis of human c-Myc locus, chicken homologue, and myelocytomatosis virus MC29 transforming gene reveals a highly conserved gene product. Proc. Natl. Acad. Sci. USA. 80:1983;3642-3645.
68. Watt R., Stanton L.W., Marcu K.B., Gallo R.C., Croce C.M., Rovera G. Nucleotide sequence of cloned cDNA of human c-Myc oncogene. Nature. 303:1983;725-728.
69. Winston R.L., Gottesfeld J.M. Rapid identification of key amino-acid-DNA contacts through combinatorial peptide synthesis. Chem. Biol. 7:2000;245-251.
70. Zervos A.S., Gyuris J., Brent R. Mxi1, a protein that specifically interacts with max to bind Myc-Max recognition sites. Cell. 72:1993;223-232.