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Volumn 332, Issue 4, 2005, Pages 965-968

Unique complex between bacterial azurin and tumor-suppressor protein p53

Author keywords

Azurin; Blue copper protein; Circular dichroism; Isothermal titration calorimetry; Protein protein interactions; Tumor suppressor protein p53

Indexed keywords

AZURIN; PROTEIN P53; TRYPTOPHAN; TUMOR SUPPRESSOR PROTEIN;

EID: 20444410796     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.05.038     Document Type: Article
Times cited : (55)

References (30)
  • 1
    • 0029845760 scopus 로고    scopus 로고
    • Structure and function of the p53 tumor suppressor gene: Clues for rational cancer therapeutic strategies
    • C.C. Harris Structure and function of the p53 tumor suppressor gene: clues for rational cancer therapeutic strategies J. Natl. Cancer Inst. 88 1996 1442 1455
    • (1996) J. Natl. Cancer Inst. , vol.88 , pp. 1442-1455
    • Harris, C.C.1
  • 2
    • 0026411154 scopus 로고
    • Copper protein structures
    • E.T. Adman Copper protein structures Adv. Protein Chem. 42 1991 145 197
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 4
    • 0037239225 scopus 로고    scopus 로고
    • Induction of apoptosis in macrophages by Pseudomonas aeruginosa azurin: Tumour-suppressor protein p53 and reactive oxygen species, but not redox activity, as critical elements in cytotoxicity
    • M. Goto, T. Yamada, K. Kimbara, J. Horner, M. Newcomb, T.K. Gupta, and A.M. Chakrabarty Induction of apoptosis in macrophages by Pseudomonas aeruginosa azurin: tumour-suppressor protein p53 and reactive oxygen species, but not redox activity, as critical elements in cytotoxicity Mol. Microbiol. 47 2003 549 559
    • (2003) Mol. Microbiol. , vol.47 , pp. 549-559
    • Goto, M.1    Yamada, T.2    Kimbara, K.3    Horner, J.4    Newcomb, M.5    Gupta, T.K.6    Chakrabarty, A.M.7
  • 5
    • 0345689559 scopus 로고    scopus 로고
    • Bacterial cupredoxin azurin and its interactions with the tumor suppressor protein p53
    • V. Punj, T.K. Das Gupta, and A.M. Chakrabarty Bacterial cupredoxin azurin and its interactions with the tumor suppressor protein p53 Biochem. Biophys. Res. Commun. 312 2003 109 114
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 109-114
    • Punj, V.1    Das Gupta, T.K.2    Chakrabarty, A.M.3
  • 6
    • 0036893444 scopus 로고    scopus 로고
    • The bacterial redox protein azurin induces apoptosis in J774 macrophages through complex formation and stabilization of the tumor suppressor protein p53
    • T. Yamada, M. Goto, V. Punj, O. Zaborina, K. Kimbara, T.K. Das Gupta, and A.M. Chakrabarty The bacterial redox protein azurin induces apoptosis in J774 macrophages through complex formation and stabilization of the tumor suppressor protein p53 Infect. Immun. 70 2002 7054 7062
    • (2002) Infect. Immun. , vol.70 , pp. 7054-7062
    • Yamada, T.1    Goto, M.2    Punj, V.3    Zaborina, O.4    Kimbara, K.5    Das Gupta, T.K.6    Chakrabarty, A.M.7
  • 9
    • 13144281835 scopus 로고    scopus 로고
    • Regulation of mammalian cell growth and death by bacterial redox proteins: Relevance to ecology and cancer therapy
    • T. Yamada, Y. Hiraoka, T.K. Das Gupta, and A.M. Chakrabarty Regulation of mammalian cell growth and death by bacterial redox proteins: relevance to ecology and cancer therapy Cell Cycle 3 2004 752 755
    • (2004) Cell Cycle , vol.3 , pp. 752-755
    • Yamada, T.1    Hiraoka, Y.2    Das Gupta, T.K.3    Chakrabarty, A.M.4
  • 11
    • 0035799321 scopus 로고    scopus 로고
    • Protein-DNA binding correlates with structural thermostability for the full-length human p53 protein
    • N.M. Nichols, and K.S. Matthews Protein-DNA binding correlates with structural thermostability for the full-length human p53 protein Biochemistry 40 2001 3847 3858
    • (2001) Biochemistry , vol.40 , pp. 3847-3858
    • Nichols, N.M.1    Matthews, K.S.2
  • 12
    • 0036415663 scopus 로고    scopus 로고
    • P53 contains large unstructured regions in its native state
    • S. Bell, C. Klein, L. Muller, S. Hansen, and J. Buchner p53 contains large unstructured regions in its native state J. Mol. Biol. 322 2002 917 927
    • (2002) J. Mol. Biol. , vol.322 , pp. 917-927
    • Bell, S.1    Klein, C.2    Muller, L.3    Hansen, S.4    Buchner, J.5
  • 13
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. a pH-induced conformational transition involves a peptide bond flip
    • H. Nar, A. Messerschmidt, R. Huber, M. van de Kamp, and G.W. Canters Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip J. Mol. Biol. 221 1991 765 772
    • (1991) J. Mol. Biol. , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 14
    • 0026642328 scopus 로고
    • Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 Å resolution
    • H. Nar, A. Messerschmidt, R. Huber, M. van de Kamp, and G.W. Canters Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 Å resolution FEBS Lett. 306 1992 119 124
    • (1992) FEBS Lett. , vol.306 , pp. 119-124
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 15
    • 0034608843 scopus 로고    scopus 로고
    • Copper triggered b-hairpin formation. Initiation site for azurin folding
    • I. Pozdnyakova, J. Guidry, and P. Wittung-Stafshede Copper triggered b-hairpin formation. Initiation site for azurin folding J. Am. Chem. Soc. 122 2000 6337 6338
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6337-6338
    • Pozdnyakova, I.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 16
    • 0034840236 scopus 로고    scopus 로고
    • Probing copper ligands in denatured Pseudomonas aeruginosa azurin: Unfolding His117Gly and His46Gly mutants
    • I. Pozdnyakova, J. Guidry, and P. Wittung-Stafshede Probing copper ligands in denatured Pseudomonas aeruginosa azurin: unfolding His117Gly and His46Gly mutants J. Biol. Inorg. Chem. 6 2001 182 188
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 182-188
    • Pozdnyakova, I.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 18
    • 0036225868 scopus 로고    scopus 로고
    • Studies of Pseudomonas aeruginosa azurin mutants: Cavities in beta-barrel do not affect refolding speed
    • I. Pozdnyakova, J. Guidry, and P. Wittung-Stafshede Studies of Pseudomonas aeruginosa azurin mutants: cavities in beta-barrel do not affect refolding speed Biophys. J. 82 2002 2645 2651
    • (2002) Biophys. J. , vol.82 , pp. 2645-2651
    • Pozdnyakova, I.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 19
    • 0035904453 scopus 로고    scopus 로고
    • Biological relevance of metal binding before protein folding
    • I. Pozdnyakova, and P. Wittung-Stafshede Biological relevance of metal binding before protein folding J. Am. Chem. Soc. 123 2001 10135 10136
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10135-10136
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 20
    • 0035856539 scopus 로고    scopus 로고
    • Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin
    • I. Pozdnyakova, and P. Wittung-Stafshede Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin Biochemistry 40 2001 13728 13733
    • (2001) Biochemistry , vol.40 , pp. 13728-13733
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 21
    • 15244355262 scopus 로고    scopus 로고
    • Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin
    • C.J. Wilson, and P. Wittung-Stafshede Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin Proc. Natl. Acad. Sci USA 102 2005 3984 3987
    • (2005) Proc. Natl. Acad. Sci USA , vol.102 , pp. 3984-3987
    • Wilson, C.J.1    Wittung-Stafshede, P.2
  • 22
    • 1242341404 scopus 로고    scopus 로고
    • Approaching the speed limit for Greek Key beta-barrel formation: Transition-state movement tunes folding rate of zinc-substituted azurin
    • I. Pozdnyakova, and P. Wittung-Stafshede Approaching the speed limit for Greek Key beta-barrel formation: transition-state movement tunes folding rate of zinc-substituted azurin Biochim. Biophys. Acta 1651 2003 1 4
    • (2003) Biochim. Biophys. Acta , vol.1651 , pp. 1-4
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 23
    • 4444289990 scopus 로고    scopus 로고
    • Conformational changes in azurin from Pseudomonas aeruginosa induced through chemical and physical protocols
    • L. Fuentes, J. Oyola, M. Fernandez, and E. Quinones Conformational changes in azurin from Pseudomonas aeruginosa induced through chemical and physical protocols Biophys. J. 87 2004 1873 1880
    • (2004) Biophys. J. , vol.87 , pp. 1873-1880
    • Fuentes, L.1    Oyola, J.2    Fernandez, M.3    Quinones, E.4
  • 26
    • 2342485664 scopus 로고    scopus 로고
    • Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin
    • J. Marks, I. Pozdnyakova, J. Guidry, and P. Wittung-Stafshede Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin J. Biol. Inorg. Chem. 9 2004 281 288
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 281-288
    • Marks, J.1    Pozdnyakova, I.2    Guidry, J.3    Wittung-Stafshede, P.4
  • 27
    • 0035914136 scopus 로고    scopus 로고
    • P53 unfolding detected by CD but not by tryptophan fluorescence
    • N.M. Nichols, and K.S. Matthews p53 unfolding detected by CD but not by tryptophan fluorescence Biochem. Biophys. Res. Commun. 288 2001 111 115
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 111-115
    • Nichols, N.M.1    Matthews, K.S.2
  • 28
    • 0028345259 scopus 로고
    • Unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy
    • G. Gilardi, G. Mei, N. Rosato, G.W. Canters, and A. Finazzi-Agro Unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy Biochemistry 33 1994 1425 1432
    • (1994) Biochemistry , vol.33 , pp. 1425-1432
    • Gilardi, G.1    Mei, G.2    Rosato, N.3    Canters, G.W.4    Finazzi-Agro, A.5
  • 30
    • 13944254720 scopus 로고    scopus 로고
    • Rusticyanin, a bacterial electron transfer protein, causes G1 arrest in J774 and apoptosis in human cancer cells
    • T. Yamada, Y. Hiraoka, T.K. Das Gupta, and A.M. Chakrabarty Rusticyanin, a bacterial electron transfer protein, causes G1 arrest in J774 and apoptosis in human cancer cells Cell Cycle 3 2004 1182 1187
    • (2004) Cell Cycle , vol.3 , pp. 1182-1187
    • Yamada, T.1    Hiraoka, Y.2    Das Gupta, T.K.3    Chakrabarty, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.