Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1993 Dec 25;21(25):5987–5996. doi: 10.1093/nar/21.25.5987

Predicted common structural features of DNA-binding domains from Ets, Myb and HMG transcription factors.

M P Laget 1, I Callebaut 1, Y de Launoit 1, D Stehelin 1, J P Mornon 1
PMCID: PMC310485  PMID: 8290361

Abstract

The Ets family of transcription factors shares a 85 amino acid domain, named the ETS domain, which appears responsible for their DNA binding activity. This domain did not show any clear similarity with already known DNA binding motifs. Hydrophobic Cluster Analysis (HCA), a sensitive method able to detect protein structural relationships even at low sequence identity, was chosen in order to compare the ETS domain with other conventional DNA binding motifs. HCA analysis combined with known three-dimensional NMR data, suggests that the ETS domain may be structurally related to the Myb DNA binding domain and possibly to the HMG one. Indeed, the ETS domain is likely to contain two helix-loop-helix motifs.

Full text

PDF
5987

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ben-David Y., Giddens E. B., Letwin K., Bernstein A. Erythroleukemia induction by Friend murine leukemia virus: insertional activation of a new member of the ets gene family, Fli-1, closely linked to c-ets-1. Genes Dev. 1991 Jun;5(6):908–918. doi: 10.1101/gad.5.6.908. [DOI] [PubMed] [Google Scholar]
  2. Bianchi M. E., Falciola L., Ferrari S., Lilley D. M. The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins. EMBO J. 1992 Mar;11(3):1055–1063. doi: 10.1002/j.1460-2075.1992.tb05144.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Billeter M., Qian Y., Otting G., Müller M., Gehring W. J., Wüthrich K. Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy. J Mol Biol. 1990 Jul 5;214(1):183–197. doi: 10.1016/0022-2836(90)90155-f. [DOI] [PubMed] [Google Scholar]
  4. Bowie J. U., Sauer R. T. TraY proteins of F and related episomes are members of the Arc and Mnt repressor family. J Mol Biol. 1990 Jan 5;211(1):5–6. doi: 10.1016/0022-2836(90)90004-6. [DOI] [PubMed] [Google Scholar]
  5. Breg J. N., van Opheusden J. H., Burgering M. J., Boelens R., Kaptein R. Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins. Nature. 1990 Aug 9;346(6284):586–589. doi: 10.1038/346586a0. [DOI] [PubMed] [Google Scholar]
  6. Brown T. A., McKnight S. L. Specificities of protein-protein and protein-DNA interaction of GABP alpha and two newly defined ets-related proteins. Genes Dev. 1992 Dec;6(12B):2502–2512. doi: 10.1101/gad.6.12b.2502. [DOI] [PubMed] [Google Scholar]
  7. Burtis K. C., Thummel C. S., Jones C. W., Karim F. D., Hogness D. S. The Drosophila 74EF early puff contains E74, a complex ecdysone-inducible gene that encodes two ets-related proteins. Cell. 1990 Apr 6;61(1):85–99. doi: 10.1016/0092-8674(90)90217-3. [DOI] [PubMed] [Google Scholar]
  8. Callebaut I., Renoir J. M., Lebeau M. C., Massol N., Burny A., Baulieu E. E., Mornon J. P. An immunophilin that binds M(r) 90,000 heat shock protein: main structural features of a mammalian p59 protein. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6270–6274. doi: 10.1073/pnas.89.14.6270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chen T., Bunting M., Karim F. D., Thummel C. S. Isolation and characterization of five Drosophila genes that encode an ets-related DNA binding domain. Dev Biol. 1992 May;151(1):176–191. doi: 10.1016/0012-1606(92)90225-6. [DOI] [PubMed] [Google Scholar]
  10. Dalton S., Treisman R. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell. 1992 Feb 7;68(3):597–612. doi: 10.1016/0092-8674(92)90194-h. [DOI] [PubMed] [Google Scholar]
  11. Diffley J. F., Stillman B. A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7864–7868. doi: 10.1073/pnas.88.17.7864. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Dudek H., Reddy E. P. Identification of two translational products for c-myb. Oncogene. 1989 Sep;4(9):1061–1066. [PubMed] [Google Scholar]
  13. Dudek H., Tantravahi R. V., Rao V. N., Reddy E. S., Reddy E. P. Myb and Ets proteins cooperate in transcriptional activation of the mim-1 promoter. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1291–1295. doi: 10.1073/pnas.89.4.1291. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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. 1992 Dec 24;71(7):1223–1237. doi: 10.1016/s0092-8674(05)80070-4. [DOI] [PubMed] [Google Scholar]
  15. Ferrari S., Harley V. R., Pontiggia A., Goodfellow P. N., Lovell-Badge R., Bianchi M. E. SRY, like HMG1, recognizes sharp angles in DNA. EMBO J. 1992 Dec;11(12):4497–4506. doi: 10.1002/j.1460-2075.1992.tb05551.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ferré-D'Amaré 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. 1993 May 6;363(6424):38–45. doi: 10.1038/363038a0. [DOI] [PubMed] [Google Scholar]
  17. Frampton J., Gibson T. J., Ness S. A., Döderlein G., Graf T. Proposed structure for the DNA-binding domain of the Myb oncoprotein based on model building and mutational analysis. Protein Eng. 1991 Dec;4(8):891–901. doi: 10.1093/protein/4.8.891. [DOI] [PubMed] [Google Scholar]
  18. Frampton J., Leutz A., Gibson T., Graf T. DNA-binding domain ancestry. Nature. 1989 Nov 9;342(6246):134–134. doi: 10.1038/342134a0. [DOI] [PubMed] [Google Scholar]
  19. Gaboriaud C., Bissery V., Benchetrit T., Mornon J. P. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 1987 Nov 16;224(1):149–155. doi: 10.1016/0014-5793(87)80439-8. [DOI] [PubMed] [Google Scholar]
  20. Giese K., Cox J., Grosschedl R. The HMG domain of lymphoid enhancer factor 1 bends DNA and facilitates assembly of functional nucleoprotein structures. Cell. 1992 Apr 3;69(1):185–195. doi: 10.1016/0092-8674(92)90129-z. [DOI] [PubMed] [Google Scholar]
  21. Golay J., Introna M., Graf T. A single point mutation in the v-ets oncogene affects both erythroid and myelomonocytic cell differentiation. Cell. 1988 Dec 23;55(6):1147–1158. doi: 10.1016/0092-8674(88)90259-0. [DOI] [PubMed] [Google Scholar]
  22. Gonda T. J., Gough N. M., Dunn A. R., de Blaquiere J. Nucleotide sequence of cDNA clones of the murine myb proto-oncogene. EMBO J. 1985 Aug;4(8):2003–2008. doi: 10.1002/j.1460-2075.1985.tb03884.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Heinz D. W., Baase W. A., Dahlquist F. W., Matthews B. W. How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature. 1993 Feb 11;361(6412):561–564. doi: 10.1038/361561a0. [DOI] [PubMed] [Google Scholar]
  24. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J. 1991 Dec 1;280(Pt 2):309–316. doi: 10.1042/bj2800309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Henrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J. P. Cellulase families revealed by hydrophobic cluster analysis. Gene. 1989 Sep 1;81(1):83–95. doi: 10.1016/0378-1119(89)90339-9. [DOI] [PubMed] [Google Scholar]
  26. Janknecht R., Nordheim A. Elk-1 protein domains required for direct and SRF-assisted DNA-binding. Nucleic Acids Res. 1992 Jul 11;20(13):3317–3324. doi: 10.1093/nar/20.13.3317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Ju Q. D., Morrow B. E., Warner J. R. REB1, a yeast DNA-binding protein with many targets, is essential for growth and bears some resemblance to the oncogene myb. Mol Cell Biol. 1990 Oct;10(10):5226–5234. doi: 10.1128/mcb.10.10.5226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Kanei-Ishii C., Sarai A., Sawazaki T., Nakagoshi H., He D. N., Ogata K., Nishimura Y., Ishii S. The tryptophan cluster: a hypothetical structure of the DNA-binding domain of the myb protooncogene product. J Biol Chem. 1990 Nov 15;265(32):19990–19995. [PubMed] [Google Scholar]
  29. Karim F. D., Urness L. D., Thummel C. S., Klemsz M. J., McKercher S. R., Celada A., Van Beveren C., Maki R. A., Gunther C. V., Nye J. A. The ETS-domain: a new DNA-binding motif that recognizes a purine-rich core DNA sequence. Genes Dev. 1990 Sep;4(9):1451–1453. doi: 10.1101/gad.4.9.1451. [DOI] [PubMed] [Google Scholar]
  30. Karim F. D., Urness L. D., Thummel C. S., Klemsz M. J., McKercher S. R., Celada A., Van Beveren C., Maki R. A., Gunther C. V., Nye J. A. The ETS-domain: a new DNA-binding motif that recognizes a purine-rich core DNA sequence. Genes Dev. 1990 Sep;4(9):1451–1453. doi: 10.1101/gad.4.9.1451. [DOI] [PubMed] [Google Scholar]
  31. Keefe L. J., Sondek J., Shortle D., Lattman E. E. The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275–3279. doi: 10.1073/pnas.90.8.3275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Kissinger C. R., Liu B. S., Martin-Blanco E., Kornberg T. B., Pabo C. O. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions. Cell. 1990 Nov 2;63(3):579–590. doi: 10.1016/0092-8674(90)90453-l. [DOI] [PubMed] [Google Scholar]
  33. Klempnauer K. H., Ramsay G., Bishop J. M., Moscovici M. G., Moscovici C., McGrath J. P., Levinson A. D. The product of the retroviral transforming gene v-myb is a truncated version of the protein encoded by the cellular oncogene c-myb. Cell. 1983 Jun;33(2):345–355. doi: 10.1016/0092-8674(83)90416-6. [DOI] [PubMed] [Google Scholar]
  34. Klempnauer K. H., Symonds G., Evan G. I., Bishop J. M. Subcellular localization of proteins encoded by oncogenes of avian myeloblastosis virus and avian leukemia virus E26 and by chicken c-myb gene. Cell. 1984 Jun;37(2):537–547. doi: 10.1016/0092-8674(84)90384-2. [DOI] [PubMed] [Google Scholar]
  35. LaMarco K., Thompson C. C., Byers B. P., Walton E. M., McKnight S. L. Identification of Ets- and notch-related subunits in GA binding protein. Science. 1991 Aug 16;253(5021):789–792. doi: 10.1126/science.1876836. [DOI] [PubMed] [Google Scholar]
  36. LaMarco K., Thompson C. C., Byers B. P., Walton E. M., McKnight S. L. Identification of Ets- and notch-related subunits in GA binding protein. Science. 1991 Aug 16;253(5021):789–792. doi: 10.1126/science.1876836. [DOI] [PubMed] [Google Scholar]
  37. Lane T., Ibanez C., Garcia A., Graf T., Lipsick J. Transformation by v-myb correlates with trans-activation of gene expression. Mol Cell Biol. 1990 Jun;10(6):2591–2598. doi: 10.1128/mcb.10.6.2591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Laudet V., Niel C., Duterque-Coquillaud M., Leprince D., Stehelin D. Evolution of the ets gene family. Biochem Biophys Res Commun. 1993 Jan 15;190(1):8–14. doi: 10.1006/bbrc.1993.1002. [DOI] [PubMed] [Google Scholar]
  39. Laudet V., Stehelin D., Clevers H. Ancestry and diversity of the HMG box superfamily. Nucleic Acids Res. 1993 May 25;21(10):2493–2501. doi: 10.1093/nar/21.10.2493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Lautenberger J. A., Burdett L. A., Gunnell M. A., Qi S., Watson D. K., O'Brien S. J., Papas T. S. Genomic dispersal of the ets gene family during metazoan evolution. Oncogene. 1992 Sep;7(9):1713–1719. [PubMed] [Google Scholar]
  41. Lemesle-Varloot L., Henrissat B., Gaboriaud C., Bissery V., Morgat A., Mornon J. P. Hydrophobic cluster analysis: procedures to derive structural and functional information from 2-D-representation of protein sequences. Biochimie. 1990 Aug;72(8):555–574. doi: 10.1016/0300-9084(90)90120-6. [DOI] [PubMed] [Google Scholar]
  42. Lemesle-Varloot L., Ojasoo T., Mornon J. P., Raynaud J. P. A model for the determination of the 3D-spatial distribution of the functions of the hormone-binding domain of receptors that bind 3-keto-4-ene steroids. J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):369–388. doi: 10.1016/0960-0760(92)90363-n. [DOI] [PubMed] [Google Scholar]
  43. Leprince D., Crepieux P., Stehelin D. c-ets-1 DNA binding to the PEA3 motif is differentially inhibited by all the mutations found in v-ets. Oncogene. 1992 Jan;7(1):9–17. [PubMed] [Google Scholar]
  44. Leprince D., Gegonne A., Coll J., de Taisne C., Schneeberger A., Lagrou C., Stehelin D. A putative second cell-derived oncogene of the avian leukaemia retrovirus E26. Nature. 1983 Nov 24;306(5941):395–397. doi: 10.1038/306395a0. [DOI] [PubMed] [Google Scholar]
  45. Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science. 1985 Mar 22;227(4693):1435–1441. doi: 10.1126/science.2983426. [DOI] [PubMed] [Google Scholar]
  46. Lüscher B., Eisenman R. N. New light on Myc and Myb. Part II. Myb. Genes Dev. 1990 Dec;4(12B):2235–2241. doi: 10.1101/gad.4.12b.2235. [DOI] [PubMed] [Google Scholar]
  47. Macleod K., Leprince D., Stehelin D. The ets gene family. Trends Biochem Sci. 1992 Jul;17(7):251–256. doi: 10.1016/0968-0004(92)90404-w. [DOI] [PubMed] [Google Scholar]
  48. Marocco A., Wissenbach M., Becker D., Paz-Ares J., Saedler H., Salamini F., Rohde W. Multiple genes are transcribed in Hordeum vulgare and Zea mays that carry the DNA binding domain of the myb oncoproteins. Mol Gen Genet. 1989 Apr;216(2-3):183–187. doi: 10.1007/BF00334354. [DOI] [PubMed] [Google Scholar]
  49. Metz T., Graf T. v-myb and v-ets transform chicken erythroid cells and cooperate both in trans and in cis to induce distinct differentiation phenotypes. Genes Dev. 1991 Mar;5(3):369–380. doi: 10.1101/gad.5.3.369. [DOI] [PubMed] [Google Scholar]
  50. Mondragón A., Wolberger C., Harrison S. C. Structure of phage 434 Cro protein at 2.35 A resolution. J Mol Biol. 1989 Jan 5;205(1):179–188. doi: 10.1016/0022-2836(89)90374-4. [DOI] [PubMed] [Google Scholar]
  51. Moreau-Gachelin F., Tavitian A., Tambourin P. Spi-1 is a putative oncogene in virally induced murine erythroleukaemias. Nature. 1988 Jan 21;331(6153):277–280. doi: 10.1038/331277a0. [DOI] [PubMed] [Google Scholar]
  52. Mornon J. P., Bissery V., Gaboriaud C., Thomas A., Ojasoo T., Raynaud J. P. Hydrophobic cluster analysis (HCA) of the hormone-binding domain of receptor proteins. J Steroid Biochem. 1989;34(1-6):355–361. doi: 10.1016/0022-4731(89)90108-8. [DOI] [PubMed] [Google Scholar]
  53. Mossing M. C., Sauer R. T. Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence. Science. 1990 Dec 21;250(4988):1712–1715. doi: 10.1126/science.2148648. [DOI] [PubMed] [Google Scholar]
  54. Nunn M. F., Seeburg P. H., Moscovici C., Duesberg P. H. Tripartite structure of the avian erythroblastosis virus E26 transforming gene. Nature. 1983 Nov 24;306(5941):391–395. doi: 10.1038/306391a0. [DOI] [PubMed] [Google Scholar]
  55. Nye J. A., Petersen J. M., Gunther C. V., Jonsen M. D., Graves B. J. Interaction of murine ets-1 with GGA-binding sites establishes the ETS domain as a new DNA-binding motif. Genes Dev. 1992 Jun;6(6):975–990. doi: 10.1101/gad.6.6.975. [DOI] [PubMed] [Google Scholar]
  56. O'Shea E. K., Rutkowski R., Kim P. S. Evidence that the leucine zipper is a coiled coil. Science. 1989 Jan 27;243(4890):538–542. doi: 10.1126/science.2911757. [DOI] [PubMed] [Google Scholar]
  57. Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., Ishii S., Nishimura Y. Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6428–6432. doi: 10.1073/pnas.89.14.6428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Ohlendorf D. H., Anderson W. F., Fisher R. G., Takeda Y., Matthews B. W. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature. 1982 Aug 19;298(5876):718–723. doi: 10.1038/298718a0. [DOI] [PubMed] [Google Scholar]
  59. Pabo C. O., Sauer R. T. Transcription factors: structural families and principles of DNA recognition. Annu Rev Biochem. 1992;61:1053–1095. doi: 10.1146/annurev.bi.61.070192.005201. [DOI] [PubMed] [Google Scholar]
  60. Parisi M. A., Clayton D. A. Similarity of human mitochondrial transcription factor 1 to high mobility group proteins. Science. 1991 May 17;252(5008):965–969. doi: 10.1126/science.2035027. [DOI] [PubMed] [Google Scholar]
  61. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Pearson W. R. Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol. 1990;183:63–98. doi: 10.1016/0076-6879(90)83007-v. [DOI] [PubMed] [Google Scholar]
  63. Pribyl L. J., Watson D. K., Schulz R. A., Papas T. S. D-elg, a member of the Drosophila ets gene family: sequence, expression and evolutionary comparison. Oncogene. 1991 Jul;6(7):1175–1183. [PubMed] [Google Scholar]
  64. Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F. Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis. Protein Eng. 1991 Feb;4(3):325–333. doi: 10.1093/protein/4.3.325. [DOI] [PubMed] [Google Scholar]
  65. Rao V. N., Huebner K., Isobe M., ar-Rushdi A., Croce C. M., Reddy E. S. elk, tissue-specific ets-related genes on chromosomes X and 14 near translocation breakpoints. Science. 1989 Apr 7;244(4900):66–70. doi: 10.1126/science.2539641. [DOI] [PubMed] [Google Scholar]
  66. Ravel-Chapuis P., Leprince D., Pain B., Li R., Domenget C., Stehelin D., Samarut J., Jurdic P. v-myb and v-ets cooperate for the mitogenic stimulation of primary fibroblasts by avian E26 retrovirus. J Virol. 1991 Jul;65(7):3928–3931. doi: 10.1128/jvi.65.7.3928-3931.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Read C. M., Cary P. D., Crane-Robinson C., Driscoll P. C., Norman D. G. Solution structure of a DNA-binding domain from HMG1. Nucleic Acids Res. 1993 Jul 25;21(15):3427–3436. doi: 10.1093/nar/21.15.3427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Reddy E. S., Rao V. N., Papas T. S. The erg gene: a human gene related to the ets oncogene. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6131–6135. doi: 10.1073/pnas.84.17.6131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Rosson D., Dugan D., Reddy E. P. Aberrant splicing events that are induced by proviral integration: implications for myb oncogene activation. Proc Natl Acad Sci U S A. 1987 May;84(10):3171–3175. doi: 10.1073/pnas.84.10.3171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Saikumar P., Murali R., Reddy E. P. Role of tryptophan repeats and flanking amino acids in Myb-DNA interactions. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8452–8456. doi: 10.1073/pnas.87.21.8452. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Schoentgen F., Seddiqi N., Bucquoy S., Jollès P., Lemesle-Varloot L., Provost K., Mornon J. P. Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling. Protein Eng. 1992 Jun;5(4):295–303. doi: 10.1093/protein/5.4.295. [DOI] [PubMed] [Google Scholar]
  72. Somers W. S., Phillips S. E. Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature. 1992 Oct 1;359(6394):387–393. doi: 10.1038/359387a0. [DOI] [PubMed] [Google Scholar]
  73. Suzuki M. Common features in DNA recognition helices of eukaryotic transcription factors. EMBO J. 1993 Aug;12(8):3221–3226. doi: 10.1002/j.1460-2075.1993.tb05991.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Tei H., Nihonmatsu I., Yokokura T., Ueda R., Sano Y., Okuda T., Sato K., Hirata K., Fujita S. C., Yamamoto D. pokkuri, a Drosophila gene encoding an E-26-specific (Ets) domain protein, prevents overproduction of the R7 photoreceptor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6856–6860. doi: 10.1073/pnas.89.15.6856. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Thompson C. B., Wang C. Y., Ho I. C., Bohjanen P. R., Petryniak B., June C. H., Miesfeldt S., Zhang L., Nabel G. J., Karpinski B. cis-acting sequences required for inducible interleukin-2 enhancer function bind a novel Ets-related protein, Elf-1. Mol Cell Biol. 1992 Mar;12(3):1043–1053. doi: 10.1128/mcb.12.3.1043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Thompson C. C., Brown T. A., McKnight S. L. Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex. Science. 1991 Aug 16;253(5021):762–768. doi: 10.1126/science.1876833. [DOI] [PubMed] [Google Scholar]
  77. Thoreau E., Petridou B., Kelly P. A., Djiane J., Mornon J. P. Structural symmetry of the extracellular domain of the cytokine/growth hormone/prolactin receptor family and interferon receptors revealed by hydrophobic cluster analysis. FEBS Lett. 1991 Apr 22;282(1):26–31. doi: 10.1016/0014-5793(91)80437-8. [DOI] [PubMed] [Google Scholar]
  78. Tice-Baldwin K., Fink G. R., Arndt K. T. BAS1 has a Myb motif and activates HIS4 transcription only in combination with BAS2. Science. 1989 Nov 17;246(4932):931–935. doi: 10.1126/science.2683089. [DOI] [PubMed] [Google Scholar]
  79. Wang C. Y., Petryniak B., Ho I. C., Thompson C. B., Leiden J. M. Evolutionarily conserved Ets family members display distinct DNA binding specificities. J Exp Med. 1992 May 1;175(5):1391–1399. doi: 10.1084/jem.175.5.1391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Waterman M. L., Fischer W. H., Jones K. A. A thymus-specific member of the HMG protein family regulates the human T cell receptor C alpha enhancer. Genes Dev. 1991 Apr;5(4):656–669. doi: 10.1101/gad.5.4.656. [DOI] [PubMed] [Google Scholar]
  81. Watson D. K., McWilliams M. J., Lapis P., Lautenberger J. A., Schweinfest C. W., Papas T. S. Mammalian ets-1 and ets-2 genes encode highly conserved proteins. Proc Natl Acad Sci U S A. 1988 Nov;85(21):7862–7866. doi: 10.1073/pnas.85.21.7862. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Weir H. M., Kraulis P. J., Hill C. S., Raine A. R., Laue E. D., Thomas J. O. Structure of the HMG box motif in the B-domain of HMG1. EMBO J. 1993 Apr;12(4):1311–1319. doi: 10.1002/j.1460-2075.1993.tb05776.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Wolberger C., Vershon A. K., Liu B., Johnson A. D., Pabo C. O. Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. Cell. 1991 Nov 1;67(3):517–528. doi: 10.1016/0092-8674(91)90526-5. [DOI] [PubMed] [Google Scholar]
  84. Woodcock S., Mornon J. P., Henrissat B. Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng. 1992 Oct;5(7):629–635. doi: 10.1093/protein/5.7.629. [DOI] [PubMed] [Google Scholar]
  85. Xin J. H., Cowie A., Lachance P., Hassell J. A. Molecular cloning and characterization of PEA3, a new member of the Ets oncogene family that is differentially expressed in mouse embryonic cells. Genes Dev. 1992 Mar;6(3):481–496. doi: 10.1101/gad.6.3.481. [DOI] [PubMed] [Google Scholar]
  86. de Vos A. M., Ultsch M., Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 1992 Jan 17;255(5042):306–312. doi: 10.1126/science.1549776. [DOI] [PubMed] [Google Scholar]
  87. van de Wetering M., Clevers H. Sequence-specific interaction of the HMG box proteins TCF-1 and SRY occurs within the minor groove of a Watson-Crick double helix. EMBO J. 1992 Aug;11(8):3039–3044. doi: 10.1002/j.1460-2075.1992.tb05374.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES