A c- Jim activation domain peptide and its corresponding phosphopeptide have potential to adopt α-heiical conformation

Peptide Research

Volumn 9, Issue 2, 1996, Pages 71-78

  John, Matthias ^a,b   Briand, Jean Paul ^a,b   Schnarr, Manfred ^a,b  

^a INSTITUT DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^b INST DE BIOL MOLEC ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE FRAGMENT; PHOSPHOPEPTIDE; PROTEIN C JUN;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; COMPARATIVE STUDY; PROTEIN SECONDARY STRUCTURE;

CIRCULAR DICHROISM; PEPTIDE FRAGMENTS; PHOSPHOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS C-JUN;

EID: 0030091668     PISSN: 10405704     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Angel, P., M. Imagawa, R. Chiu, B. Stein, R.J. Imbra, H.J. Rahmsdorf, C. Jonat, P. Herrlich and M. Karin. 1987. Phorbol ester inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor. Cell 49:729-739.
2. Angel, P. and M. Karin. 1991. The role of Jun, Fos and AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1072:129-157.
3. Angel, P., T. Smcal, J. Meek and M. Karin. 1989. Jun and v-Jun contain multiple regions that participate in transcriptional activation in an interdépendant manner. New Biol. 1:35-43.
4. Arias, J., A.S. Alberts, P. Brindle, F.-X. Claret, T. Smeal, M. Karin, J. Feramisco and M. Montminy. 1994. Activation of cAMP and mitogen responsive genes relies on a common nuclear factor. Nature 570:226-229.
5. Bannister, A.J., T. Oehler, D. Wilhelm, P. Angel and T. Kouzarides. 1995. Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro. Oncogene 11:2509-2514.
6. Baxevanis, A.D. and C.R. Vinson. 1993. Interactions of coiled coils in transcription factors: where is the specificity? Curr. Opin. Genet. Dev. 3:278-285.
7. 1. Evidence of trifluoroethanol induced native-like β-hairpin formation. Biochemistry 33:6004-6014.
8. Bohmann, D., T.J. Bos, A. Admon, T. Nishimura, P.K. Vogt and R. Tjian. 1987. Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-I. Science 238:1386-1392
9. Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer D. and Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 575:377-382.
10. Busch, S.J. and P. Sassone-Corsi. 1990. Dimers, leucine zippers and DNA binding domains. Trends Gen. 6:36-40.
11. Chen, Y.-H., J.T. Yang and K.H. Chau. 1974. Determination of the helix and form of proteins in aqueous solution by circular dichroism. Biochemistry 13:3350-3359.
12. Chou, P.Y. and G.D. Fasman. 1978. Empirical predictions of protein conformation. Ann. Rev. Biochem. 47:251-276.
13. Coso, O.A., M. Chiariello, J.-C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki and J.S. Gutkind. 1995. The small GTP-binding proteins Racl and Cdc42 regulate the activity of the JNK/SAPK signalling pathway. Cell 81:l 137-1146.
14. Dahlman-Wright. K., H. Baumann, I.J. McEwan, T. Almlöf, A.P.H. Wright, J.-Å. Gustafsson and T. Hard. 1995. Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor. Proc. Natl. Acad. Sci. 92:1699-1703.
15. Dérijard, B., M. Hibi, I.-H. Wu, T. Barrett, B. Su, T. Deng, M. Karin and R.J. Davis. 1994. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037.
16. Donaldson, L. and J.P. Capone. 1992. Purification and characterization of the carboxylterminal transactivation domain of Vmw65 from herpes simplex virus type I. i. Biol. Chem. 267:1411-1414.
17. Garnier, J., D.J. Osguthorpe and B. Rob-son. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:97-120.
18. Glover, M.J.N. and S.C. Harrison. 1995. Crystal structure of the heterodimeric bZip transcription factor c-Fos-c-Jun bound to DNA. Nature 573:257-261.
19. Hahn, S. 1993. Structure (?) and function of acidic transcription activators. Cell 72:481-483.
20. Hollosi, M., L. Urge, A. Perczel, J. Kajtâr, I. Teplân, L. Ötvös Jr. and G.D. Fasman. 1992. Metal ion-induced conformational changes of phosphorylated fragments of human neurofilament (NF-M) protein. J. Mol. Biol. 223:673-682.
21. Hudson, D. 1988. Methological implications of simultaneous solid-phase peptide synthesis. I. Comparison of different coupling procedures. J. Org. Chem. 53:617-624.
22. Hurst, H. 1994. Transcription factors 1: bZIP proteins. Protein Profile 1:123-166.
23. Jasanoff, A. and A.R. Fersht. 1994. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33:2129-2135.
24. Kallunki, T., B. Su, I. Tsigelny, H.K. Sluss, B. Dérijard, G. Moore, R.J. Davis and M. Karin. 1994. JNK2 contains a specificity-determining region responsible for efficient cJun binding and phosphorylation. Genes Dev. 8:2996-3007.
25. Karin, M. 1995. The regulation of AP-1 activity by mitogen-activated protein kinases. J. Biol. Chem. 270:16483-16486.
26. Kemmik, J. and T.E. Creighton. 1995. Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor. Biochemistry 34:12630-12635.
27. King, D., C. Fields and G. Fields. 1990. A cleavage method which minimizes side reactions following Fmoc solid-phase peptide synthesis. Int. J. Pept. Protein Res. 36:255-266.
28. Lee,W., A. Haslinger, M. Karin and R. Tjian. 1987. Activation of transcription by two factors that bind promotor and enhancer sequences of the human metallothionein gene and SV40. Nature 325:368-372.
29. Lacombe, J.M., F. Andriamanampisoa and A.A. Pavia. 1990. Solid-phase synthesis of peptides containing phosphoserine using phosphate tert.-butyl protecting group. Int. J. Pept. Protein Res. 36:275-280.
30. Lang, E., G.I. Szendrei, I. Elekes, V.M.-Y. Lee and L. Otvos Jr. 1992. Reversible pleated sheet formation of a phosphorylated synthetic t peptide. Biochem. Biophys. Res. Commun. 182:63-69.
31. Leuther, K.K., J.M. Salmeron and S.A. Johnston. 1993. Genetic evidence that an activation domain of GAL4 does not require acidity and may form ̀-sheet. Cell 72:595-606.
32. Minden, A., A. Lin, F.-X. Claret, A. Abo and M. Karin. 1995. Selective activation of the INK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
33. Neimark,J.andJ.P.Briand. 1993. Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability. Peptide Res. 6:219-228.
34. 1H-NMR. Biochemistry 31:4150-4156.
35. Otvos Jr., L., G.I. Szendrei, L. Gorbics and L. Urge. 1995. Synthesis, analysis and conformation of glycopeptides and phosphopeptides, p. 147-158. In N.D. Zcgers. W.J.A. Boersma and E. Claasen (Eds.), Immunological Recognition of Peptides in Medicine and Biology. CRC Press. Boca Raton.
36. Papavassiliou, A.G., M. Treier and D. Bohmann. 1995. Intramolecular signal transduction in c-Jun. EMBO J. 14:2014-2019.
37. Schmitz, M.L., M.A. dos Santos Suva, H. Altmann, M. Czisch, T.A. Holak and P.A. Baeuerle. 1994. Structural and functional analysis of the NF-κB p65 terminus. J. Biol. Chem. 269:25613-25620.
38. Scopes, R.K. 1974. Measurement of protein by specrophotometry at 205nm. Anal. Biochem. 59:277-282.
39. Smeal, T., B. Binetruy, D.A. Mercola, M. Birrer and M. Karin. 1991. Oncogenic and transcriptional cooperation with Ha-ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 354:494-496.
40. Sutherland, J.A., A. Cook, A.J. Bannister and T. Kouzarides. 1993. Conserved motifs in Fos and Jun define a new class of activation domain. Genes Dev. 6:1810-1819.
41. Terzi, E., L. Poteur and E. Trifilieff. 1992 Evidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysis. FEES Lett. 309:413-416.
42. Van Hoy, M., K.K. Leather, T. Kodadek and S.A. Johnston. 1993. The acidic activation domains of GCN4 and GAL4 proteins are not α-helical but form β-sheets. Cell 72:587-594.
43. Wakamiya, T., K. Saruta, J. Yasuoka and S. Kusumoto. 1994. An efficient procedure for solid-phase synthesis of phosphopeptides by the Fmoc strategy. Chem. Lett. (Japan): 1099-1102.
44. Wurtz, J.-M., W. Bourguet, J.-P. Renaud, V. Vivat, P. Chambon, D. Moras and H. Gonemeyer. 1996. A canonical structure for the ligand binding domain of nuclear receptors. Nature Struct. Biol. 3:87-94.