Evaluation of transcriptional activity of p53 in individual living mammalian cells

Analytical Biochemistry

Volumn 387, Issue 2, 2009, Pages 249-256

  Imagawa, Toshiaki ^a   Terai, Tomoko ^a   Yamada, Yoshifumi ^b   Kamada, Rui ^a   Sakaguchi, Kazuyasu ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b OLYMPUS CORPORATION   (Japan)

Author keywords

Dual reporter system; p53; Tetramer; Transcriptional activity; Tumor suppressor protein

Indexed keywords

CELLS; CYTOLOGY; FLUORESCENCE; MAMMALS; MONOMERS;

ENHANCED GREEN FLUORESCENT PROTEIN; FLUORESCENCE INTENSITY DISTRIBUTION ANALYSIS; PHYSIOLOGICAL CONCENTRATIONS; RED FLUORESCENT PROTEINS; REPORTER SYSTEMS; TETRAMERS; TRANSCRIPTIONAL ACTIVITY; TUMOR SUPPRESSOR PROTEINS;

PROTEINS;

CELL EXTRACT; DOXORUBICIN; GREEN FLUORESCENT PROTEIN; MONOMER; MUTANT PROTEIN; PROTEIN P53; RED FLUORESCENT PROTEIN; TETRAMER; TUMOR SUPPRESSOR PROTEIN;

ARTICLE; CELL LINE; CORRELATION ANALYSIS; EXPRESSION VECTOR; FLUORESCENCE; GENE MUTATION; HUMAN; HUMAN CELL; MAMMAL CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; TRANSCRIPTION REGULATION; ULTRAVIOLET RADIATION;

MAMMALIA;

EID: 61849097779     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.01.030     Document Type: Article

References (33)

1. Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 88 (1997) 323-331
2. Sakamoto H., Lewis M.S., Kodama H., Appella E., and Sakaguchi K. Specific sequences from the carboxyl terminus of human p53 gene product form anti-parallel tetramers in solution. Proc. Natl. Acad. Sci. USA 91 (1994) 8974-8978
3. Appella E., and Anderson C.W. Post-translational modifications and activation of p53 by genotoxic stresses. Eur. J. Biochem. 268 (2001) 2764-2772
4. Sakaguchi K., Herrera J.E., Saito S., Miki T., Bustin M., Vassilev A., Anderson C.W., and Appella E. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12 (1998) 2831-2841
5. Ashcroft M., Kubbutat M.H., and Vousden K.H. Regulation of p53 function and stability by phosphorylation. Mol. Cell. Biol. 19 (1999) 1751-1758
6. Barlev N.A., Liu L., Chehab N.H., Mansfield K., Harris K.G., Halazonetis T.D., and Berger S.L. Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases. Mol. Cell 8 (2001) 1243-1254
7. Zheng H., You H., Zhou X.Z., Murray S.A., Uchida T., Wulf G., Gu L., Tang X., Lu K.P., and Xiao Z.X. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response. Nature 419 (2002) 849-853
8. Zacchi P., Gostissa M., Uchida T., Salvagno C., Avolio F., Volinia S., Ronai Z., Blandino G., Schneider C., and Del Sal G. The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults. Nature 419 (2002) 853-857
9. Chukov S., Kurash J.K., Wilson J.R., Xiao B., Justin N., Ivanov G.S., McKinney K., Tempst P., Prives C., Gamblin S.J., Barlev N.A., and Reinberg D. Regulation of p53 activity through lysine methylation. Nature 432 (2004) 353-360
10. Shieh S.Y., Ikeda M., Taya Y., and Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91 (1997) 325-334
11. Momand J., Wu H.H., and Dasgupta G. MDM2: master regulator of the p53 tumor suppressor protein. Gene 242 (2000) 15-29
12. Brooks C.L., and Gu W. Ubiquitination, phosphorylation, and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15 (2003) 164-171
13. Gostissa M., Hengstermann A., Fogal V., Sandy P., Schwarz S.E., Scheffner M., and Del Sal G. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. EMBO J. 18 (1999) 6462-6471
14. Pietenpol J.A., Tokino T., Thiagalingam S., el-Deiry W.S., Kinzler K.W., and Vogelstein B. Sequence-specific transcriptional activation is essential for growth suppression by p53. Proc. Natl. Acad. Sci. USA 91 (1994) 1998-2002
15. Lee W., Harvey T.S., Yin Y., Yau P., Litchfield D., and Arrowsmith C.H. Solution structure of the tetrameric minimum transforming domain of p53. Nat. Struct. Biol. 1 (1994) 877-890
16. Clore G.M., Ernst J., Clubb R., Omichinski J.G., Kennedy W.M.P., Sakaguchi K., Appella E., and Gronenborn A.M. Refined solution structure of the oligomerization domain of the tumor suppressor p53. Nat. Struct. Biol. 2 (1995) 321-333
17. Jeffrey P.D., Gorina S., and Pavletich N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267 (1995) 1498-1502
18. Mittl P.R.E., Chene P., and Grutter M.G. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr. D 54 (1998) 86-89
19. Kuszewski J., Gronenborn A.M., and Clore G.M. Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration. J. Am. Chem. Soc. 121 (1999) 2337-2338
20. Davison T.S., Yin P., Nie E., Kay C., and Arrowsmith C.H. Characterization of the oligomerization defects of two p53 mutants found in families with Li ± Fraumeni and Li ± Fraumeni-like syndrome. Oncogene 17 (1998) 651-656
21. Mateu M.G., and Fersht A.R. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. EMBO J. 17 (1998) 2748-2758
22. Lee A.S., Galea C., DiGiammarino E.L., Jun B., Murti G., Ribeiro R.C., Zambetti G., Schultz C.P., and Kriwacki R.W. Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutant. J. Mol. Biol. 327 (2003) 699-709
23. Higashimoto Y., Asanomi Y., Takakusaki S., Lewis M.S., Uosaki K.M., Durell S.R., Anderson C.W., Appella E., and Sakaguchi K. Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer. Biochemistry 45 (2006) 1608-1619
24. Ishioka C., Shimodaira H., Englert C., Shimada A., Osada M., Jia L.Q., Suzuki T., Gamo M., and Kanamaru R. Oligomerization is not essential for growth suppression by p53 in p53-deficient osteosarcoma Saos-2 cells. Biochem. Biophys. Res. Commun. 232 (1997) 54-60
25. Kato S., Han S.Y., Liu W., Otsuka K., Shibata H., Kanamaru R., and Ishioka C. Understanding the function-structure and function-mutation relationships of p53 tumor suppressor protein by high-resolution missense mutation analysis. Proc. Natl. Acad. Sci. USA 100 (2003) 8424-8429
26. Kawaguchi T., Kato S., Otsuka K., Watanabe G., Kumabe T., Tominaga T., Yoshimoto T., and Ishioka C. The relationship among p53 oligomer formation, structure, and transcriptional activity using a comprehensive missense mutation library. Oncogene 24 (2005) 6976-6981
27. B.Y. Tao, K.C.P. Lee, in: H.G. Griffn, A.M. Griffin (Eds.), PCR Technology: Current Innovations, CRC Press, Boca Raton, FL, 1994, pp. 69-83.
28. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-termination inhibitors. Proc. Natl. Acad. Sci USA 74 (1977) 5463-5467
29. Kask P., Palo K., Ullmann D., and Gall K. Fluorescence-intensity distribution analysis and its application in biomolecular detection technology. Proc. Natl. Acad. Sci. USA 96 (1999) 13756-13761
30. Saffarian S., Li Y., Elson E.L., and Pike L.J. Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys. J. 93 (2007) 1021-1031
31. Cho Y., Gorina S., Jeffrey P.D., and Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265 (1994) 346-355
32. Bullock A.N., Henckel J., DeDecker B.S., Johnson C.M., Nikolova P.V., Proctor M.R., Lane D.P., and Fersht A.R. Thermodynamic stability of wild-type and mutant p53 core domain. Proc. Natl. Acad. Sci. USA 94 (1997) 14338-14342
33. Wong K.-B., DeDecker B.S., Freund S.M.V., Proctor M.R., Bycroft M., and Fersht A.R. Hot-spot mutants of p53 core domain evince characteristic local structural changes. Proc. Natl. Acad. Sci. USA 96 (1999) 8438-8442