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Volumn 292, Issue 22, 2017, Pages 9345-9357

Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODIFICATION; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; LIGHT SCATTERING; NUCLEIC ACIDS; PROTEINS; RNA; TRANSMISSION ELECTRON MICROSCOPY; TUMORS;

EID: 85020253860     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.762096     Document Type: Article
Times cited : (51)

References (71)
  • 2
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives, C., and Hall, P. (1999) The p53 pathway. J. Pathol. 187, 112-126
    • (1999) J. Pathol. , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.2
  • 3
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B., Lane, D., and Levine, A. J. (2000) Surfing the p53 network. Nature 408, 307-310
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 6
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger, A. C., and Fersht, A. R. (2008) Structural biology of the tumor suppressor p53. Annu. Rev. Biochem. 77, 557-582
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 7
    • 80053015725 scopus 로고    scopus 로고
    • P53 Isoforms: An intracellular microprocessor?
    • Khoury, M. P., and Bourdon, J.-C. (2011) p53 Isoforms: an intracellular microprocessor? Genes Cancer 2, 453-465
    • (2011) Genes Cancer , vol.2 , pp. 453-465
    • Khoury, M.P.1    Bourdon, J.-C.2
  • 8
    • 78650029658 scopus 로고    scopus 로고
    • The RNA helicase p68 modulates expression and function of the Δ133 isoform(s) of p53 and is inversely associated with Δ133p53 expression in breast cancer
    • Moore, H. C., Jordan, L. B., Bray, S. E., Baker, L., Quinlan, P. R., Purdie, C. A., Thompson, A. M., Bourdon, J.-C., and Fuller-Pace, F. V. (2010) The RNA helicase p68 modulates expression and function of the Δ133 isoform(s) of p53 and is inversely associated with Δ133p53 expression in breast cancer. Oncogene 29, 6475-6484
    • (2010) Oncogene , vol.29 , pp. 6475-6484
    • Moore, H.C.1    Jordan, L.B.2    Bray, S.E.3    Baker, L.4    Quinlan, P.R.5    Purdie, C.A.6    Thompson, A.M.7    Bourdon, J.-C.8    Fuller-Pace, F.V.9
  • 9
    • 85020274161 scopus 로고    scopus 로고
    • Δ113p53/Δ133p53 converts P53 from a repressor to a promoter of DNA double-stand break repair
    • Gong, L., and Chen, J. (2016) Δ113p53/Δ133p53 converts P53 from a repressor to a promoter of DNA double-stand break repair. Mol. Cell Oncol. 3, e1033587
    • (2016) Mol. Cell Oncol. , vol.3 , pp. e1033587
    • Gong, L.1    Chen, J.2
  • 10
    • 77957370163 scopus 로고    scopus 로고
    • Differential regulation of p53 function by the N-terminal Δnp53 and Δ113p53 isoforms in zebrafish embryos
    • Davidson, W. R., Kari, C., Ren, Q., Daroczi, B., Dicker, A. P., and Rodeck, U. (2010) Differential regulation of p53 function by the N-terminal ΔNp53 and Δ113p53 isoforms in zebrafish embryos. BMC Dev. Biol. 10, 102
    • (2010) BMC Dev. Biol. , vol.10 , pp. 102
    • Davidson, W.R.1    Kari, C.2    Ren, Q.3    Daroczi, B.4    Dicker, A.P.5    Rodeck, U.6
  • 11
    • 77956935083 scopus 로고    scopus 로고
    • P53 isoforms gain functions
    • Olivares-Illana, V., and Fåhraeus, R. (2010) p53 isoforms gain functions. Oncogene 29, 5113-5119
    • (2010) Oncogene , vol.29 , pp. 5113-5119
    • Olivares-Illana, V.1    Fåhraeus, R.2
  • 12
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia, A. J., and Kastan, M. B. (1998) The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev. 12, 2973-2983
    • (1998) Genes Dev. , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 14
    • 0027109075 scopus 로고
    • P53, guardian of the genome
    • Lane, D. P. (1992) p53, guardian of the genome. Nature 358, 15-16
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 15
    • 0036415663 scopus 로고    scopus 로고
    • P53 contains large unstructured regions in its native state
    • Bell, S., Klein, C., Müller, L., Hansen, S., and Buchner, J. (2002) p53 contains large unstructured regions in its native state. J. Mol. Biol. 322, 917-927
    • (2002) J. Mol. Biol. , vol.322 , pp. 917-927
    • Bell, S.1    Klein, C.2    Müller, L.3    Hansen, S.4    Buchner, J.5
  • 16
    • 0037591875 scopus 로고    scopus 로고
    • Kinetic instability of p53 core domain mutants: Implications for rescue by small molecules
    • Friedler, A., Veprintsev, D. B., Hansson, L. O., and Fersht, A. R. (2003) Kinetic instability of p53 core domain mutants: implications for rescue by small molecules. J. Biol. Chem. 278, 24108-24112
    • (2003) J. Biol. Chem. , vol.278 , pp. 24108-24112
    • Friedler, A.1    Veprintsev, D.B.2    Hansson, L.O.3    Fersht, A.R.4
  • 17
    • 0037418548 scopus 로고    scopus 로고
    • Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain
    • Butler, J. S., and Loh, S. N. (2003) Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain. Biochemistry 42, 2396-2403
    • (2003) Biochemistry , vol.42 , pp. 2396-2403
    • Butler, J.S.1    Loh, S.N.2
  • 19
    • 84896957772 scopus 로고    scopus 로고
    • The aggregation of mutant p53 produces prion-like properties in cancer
    • Rangel, L. P., Costa, D. C., Vieira, T. C., and Silva, J. L. (2014) The aggregation of mutant p53 produces prion-like properties in cancer. Prion 8, 75-84
    • (2014) Prion , vol.8 , pp. 75-84
    • Rangel, L.P.1    Costa, D.C.2    Vieira, T.C.3    Silva, J.L.4
  • 21
    • 84879751760 scopus 로고    scopus 로고
    • P53 Aggregates penetrate cells and induce the co-aggregation of intracellular p53
    • Forget, K. J., Tremblay, G., and Roucou, X. (2013) p53 Aggregates penetrate cells and induce the co-aggregation of intracellular p53. PLoS ONE 8, e69242
    • (2013) PLoS ONE , vol.8 , pp. e69242
    • Forget, K.J.1    Tremblay, G.2    Roucou, X.3
  • 24
    • 84979582295 scopus 로고    scopus 로고
    • The "Jekyll and Hyde" actions of nucleic acids on the prion-like aggregation of proteins
    • Silva, J. L., and Cordeiro, Y. (2016) The "Jekyll and Hyde" actions of nucleic acids on the prion-like aggregation of proteins. J. Biol. Chem. 291, 15482-15490
    • (2016) J. Biol. Chem. , vol.291 , pp. 15482-15490
    • Silva, J.L.1    Cordeiro, Y.2
  • 27
    • 3042664521 scopus 로고    scopus 로고
    • Binding of RNA to p53 regulates its oligomerization and DNA-binding activity
    • Yoshida, Y., Izumi, H., Torigoe, T., Ishiguchi, H., Yoshida, T., Itoh, H., and Kohno, K. (2004) Binding of RNA to p53 regulates its oligomerization and DNA-binding activity. Oncogene 23, 4371-4379
    • (2004) Oncogene , vol.23 , pp. 4371-4379
    • Yoshida, Y.1    Izumi, H.2    Torigoe, T.3    Ishiguchi, H.4    Yoshida, T.5    Itoh, H.6    Kohno, K.7
  • 28
    • 35548983482 scopus 로고    scopus 로고
    • P53 RNA interactions: New clues in an old mystery
    • Riley, K. J., and Maher, L. J., 3rd (2007) p53 RNA interactions: new clues in an old mystery. RNA 13, 1825-1833
    • (2007) RNA , vol.13 , pp. 1825-1833
    • Riley, K.J.1    Maher, L.J.2
  • 31
    • 0029907769 scopus 로고    scopus 로고
    • Filling in the blanks in the p53 protein structure
    • Pennisi, E. (1996) Filling in the blanks in the p53 protein structure. Science 274, 921-922
    • (1996) Science , vol.274 , pp. 921-922
    • Pennisi, E.1
  • 33
    • 84923693827 scopus 로고    scopus 로고
    • Mechanism of initiation of aggregation of p53 revealed by φ-value analysis
    • Wang, G., and Fersht, A. R. (2015) Mechanism of initiation of aggregation of p53 revealed by φ-value analysis. Proc. Natl. Acad. Sci. U.S.A. 112, 2437-2442
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 2437-2442
    • Wang, G.1    Fersht, A.R.2
  • 34
  • 35
    • 77953865084 scopus 로고    scopus 로고
    • (Lakowicz, J. R., ed), Springer US, Boston, MA 10.1007/978-0-387-46312-4
    • Lakowicz, J. R. (2006) Principles of Fluorescence Spectroscopy (Lakowicz, J. R., ed), Springer US, Boston, MA 10.1007/978-0-387-46312-4
    • (2006) Principles of Fluorescence Spectroscopy
    • Lakowicz, J.R.1
  • 37
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • Munishkina, L. A., and Fink, A. L. (2007) Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins. Biochim. Biophys. Acta 1768, 1862-1885
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 39
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to amyloid fibrils
    • Biancalana, M., and Koide, S. (2010) Molecular mechanism of thioflavin-T binding to amyloid fibrils. Biochim. Biophys. Acta 1804, 1405-1412
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 40
    • 84965088109 scopus 로고    scopus 로고
    • Thioflavin T as a fluorescence probe for monitoring RNA metabolism at molecular and cellular levels
    • Sugimoto, S., Arita-Morioka, K.-I., Mizunoe, Y., Yamanaka, K., and Ogura, T. (2015) Thioflavin T as a fluorescence probe for monitoring RNA metabolism at molecular and cellular levels. Nucleic Acids Res. 43, e92
    • (2015) Nucleic Acids Res. , vol.43 , pp. e92
    • Sugimoto, S.1    Arita-Morioka, K.-I.2    Mizunoe, Y.3    Yamanaka, K.4    Ogura, T.5
  • 41
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 42
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe, C. G. (2004) Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem. Sci. 29, 542-547
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 542-547
    • Glabe, C.G.1
  • 43
    • 39949084677 scopus 로고    scopus 로고
    • Intriguing nucleic-acid-binding features of mammalian prion protein
    • Silva, J. L., Lima, L. M., Foguel, D., and Cordeiro, Y. (2008) Intriguing nucleic-acid-binding features of mammalian prion protein. Trends Biochem. Sci. 33, 132-140
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 132-140
    • Silva, J.L.1    Lima, L.M.2    Foguel, D.3    Cordeiro, Y.4
  • 44
    • 77951237351 scopus 로고    scopus 로고
    • PrP interactions with nucleic acids and glycosaminoglycans in function and disease
    • Silva, J. L., Gomes, M. P., Vieira, T. C., and Cordeiro, Y. (2010) PrP interactions with nucleic acids and glycosaminoglycans in function and disease. Front. Biosci. (Landmark Ed) 15, 132-150
    • (2010) Front. Biosci. (Landmark Ed) , vol.15 , pp. 132-150
    • Silva, J.L.1    Gomes, M.P.2    Vieira, T.C.3    Cordeiro, Y.4
  • 46
    • 80051908695 scopus 로고    scopus 로고
    • Nucleic acid-mediated protein aggregation and assembly
    • Liu, C., and Zhang, Y. (2011) Nucleic acid-mediated protein aggregation and assembly. Adv. Protein Chem. Struct. Biol. 84, 1-40
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.84 , pp. 1-40
    • Liu, C.1    Zhang, Y.2
  • 47
    • 84897820467 scopus 로고    scopus 로고
    • Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases
    • 10.1007/s12551-013-0132-0
    • Cordeiro, Y., Macedo, B., Silva, J. L., and Gomes, M. P. B. (2014) Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases. Biophys. Rev. 6, 97-110 10.1007/s12551-013-0132-0
    • (2014) Biophys. Rev. , vol.6 , pp. 97-110
    • Cordeiro, Y.1    Macedo, B.2    Silva, J.L.3    Gomes, M.P.B.4
  • 48
    • 0036606348 scopus 로고    scopus 로고
    • 23S rRNA assisted folding of cytoplasmic malate dehydrogenase is distinctly different from its self-folding
    • Sanyal, S. C., Pal, S., Chowdhury, S., and DasGupta, C., and Chaudhuri, S. (2002) 23S rRNA assisted folding of cytoplasmic malate dehydrogenase is distinctly different from its self-folding. Nucleic Acids Res. 30, 2390-2397
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2390-2397
    • Sanyal, S.C.1    Pal, S.2    Chowdhury, S.3    DasGupta, C.4    Chaudhuri, S.5
  • 49
    • 0028227079 scopus 로고
    • Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes
    • Chattopadhyay, S., Das, B., Bera, A. K., Dasgupta, D., and Dasgupta, C. (1994) Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes. Biochem. J. 300, 717-721
    • (1994) Biochem. J. , vol.300 , pp. 717-721
    • Chattopadhyay, S.1    Das, B.2    Bera, A.K.3    Dasgupta, D.4    Dasgupta, C.5
  • 51
    • 79955063817 scopus 로고    scopus 로고
    • Mode of action of the antiprion drugs 6AP and GA on ribosome assisted protein folding
    • Reis, S. D., Pang, Y., Vishnu, N., Voisset, C., Galons, H., Blondel, M., and Sanyal, S. (2011) Mode of action of the antiprion drugs 6AP and GA on ribosome assisted protein folding. Biochimie 93, 1047-1054
    • (2011) Biochimie , vol.93 , pp. 1047-1054
    • Reis, S.D.1    Pang, Y.2    Vishnu, N.3    Voisset, C.4    Galons, H.5    Blondel, M.6    Sanyal, S.7
  • 53
    • 84908245287 scopus 로고    scopus 로고
    • Protein folding activity of the ribosome (PFAR): A target for antiprion compounds
    • Banerjee, D., and Sanyal, S. (2014) Protein folding activity of the ribosome (PFAR): a target for antiprion compounds. Viruses 6, 3907-3924
    • (2014) Viruses , vol.6 , pp. 3907-3924
    • Banerjee, D.1    Sanyal, S.2
  • 55
    • 15944399100 scopus 로고    scopus 로고
    • The hypothesis of the catalytic action of nucleic acid on the conversion of prion protein
    • Cordeiro, Y., and Silva, J. L. (2005) The hypothesis of the catalytic action of nucleic acid on the conversion of prion protein. Protein Pept. Lett. 12, 251-255
    • (2005) Protein Pept. Lett. , vol.12 , pp. 251-255
    • Cordeiro, Y.1    Silva, J.L.2
  • 56
    • 34547481020 scopus 로고    scopus 로고
    • Nanoparticles as catalysts for protein fibrillation
    • Colvin, V. L., and Kulinowski, K. M. (2007) Nanoparticles as catalysts for protein fibrillation. Proc. Natl. Acad. Sci. U.S.A. 104, 8679-8680
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8679-8680
    • Colvin, V.L.1    Kulinowski, K.M.2
  • 59
    • 0032746279 scopus 로고    scopus 로고
    • Complementary role of two fragments of domain v of 23 S ribosomal RNA in protein folding
    • Pal, S., Chandra, S., Chowdhury, S., Sarkar, D., Ghosh, A. N., and Gupta, C. D. (1999) Complementary role of two fragments of domain V of 23 S ribosomal RNA in protein folding. J. Biol. Chem. 274, 32771-32777
    • (1999) J. Biol. Chem. , vol.274 , pp. 32771-32777
    • Pal, S.1    Chandra, S.2    Chowdhury, S.3    Sarkar, D.4    Ghosh, A.N.5    Gupta, C.D.6
  • 61
    • 84900546902 scopus 로고    scopus 로고
    • The ribosome can prevent aggregation of partially folded protein intermediates: Studies using the Escherichia coli ribosome
    • Pathak, B. K., Mondal, S., Ghosh, A. N., and Barat, C. (2014) The ribosome can prevent aggregation of partially folded protein intermediates: studies using the Escherichia coli ribosome. PLoS ONE 9, e96425
    • (2014) PLoS ONE , vol.9 , pp. e96425
    • Pathak, B.K.1    Mondal, S.2    Ghosh, A.N.3    Barat, C.4
  • 64
    • 84978755680 scopus 로고    scopus 로고
    • Role of p53 isoforms and aggregations in cancer
    • Kim, S., and An, S. S. (2016) Role of p53 isoforms and aggregations in cancer. Medicine 95, e3993
    • (2016) Medicine , vol.95 , pp. e3993
    • Kim, S.1    An, S.S.2
  • 65
    • 84895828901 scopus 로고    scopus 로고
    • The relative mRNA expression of p53 isoforms in breast cancer is associated with clinical features and outcome
    • Avery-Kiejda, K. A., Morten, B., Wong-Brown, M. W., Mathe, A., and Scott, R. J. (2014) The relative mRNA expression of p53 isoforms in breast cancer is associated with clinical features and outcome. Carcinogenesis 35, 586-596
    • (2014) Carcinogenesis , vol.35 , pp. 586-596
    • Avery-Kiejda, K.A.1    Morten, B.2    Wong-Brown, M.W.3    Mathe, A.4    Scott, R.J.5
  • 67
    • 84891854140 scopus 로고    scopus 로고
    • Spectroscopic and DFT studies on 6-Aminophenanthridine and its derivatives provide insights in their activity towards ribosomal RNA
    • Banerjee, D., Vovusha, H., Pang, Y., Oumata, N., Sanyal, B., and Sanyal, S. (2014) Spectroscopic and DFT studies on 6-Aminophenanthridine and its derivatives provide insights in their activity towards ribosomal RNA. Biochimie 97, 194-199
    • (2014) Biochimie , vol.97 , pp. 194-199
    • Banerjee, D.1    Vovusha, H.2    Pang, Y.3    Oumata, N.4    Sanyal, B.5    Sanyal, S.6
  • 68
    • 84955499469 scopus 로고    scopus 로고
    • Molecular mechanism of viomycin inhibition of peptide elongation in bacteria
    • Holm, M., Borg, A., Ehrenberg, M., and Sanyal, S. (2016) Molecular mechanism of viomycin inhibition of peptide elongation in bacteria. Proc. Natl. Acad. Sci. U.S.A. 113, 978-983
    • (2016) Proc. Natl. Acad. Sci. U.S.A. , vol.113 , pp. 978-983
    • Holm, M.1    Borg, A.2    Ehrenberg, M.3    Sanyal, S.4
  • 69
    • 0034670221 scopus 로고    scopus 로고
    • Cryo transmission electron microscopy of liposomes and related structures
    • Almgren, M., Edwards, K., and Karlsson, G. (2000) Cryo transmission electron microscopy of liposomes and related structures. Colloids and Surfaces 174, 3-21
    • (2000) Colloids and Surfaces , vol.174 , pp. 3-21
    • Almgren, M.1    Edwards, K.2    Karlsson, G.3


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