Structural characteristics of the hydrophobic patch of azurin and its interaction with p53: A site-directed spin labeling study

Science China Life Sciences

Volumn 53, Issue 10, 2010, Pages 1181-1188

  Xu, Chao ^a,b   Yin, Jun Jie ^c   Zhao, Bao Lu ^a,b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

Author keywords

anticancer; azurin; ESR; p53; protein protein interaction; spin label

Indexed keywords

ANTINEOPLASTIC AGENT; AZURIN; MUTANT PROTEIN; PROTEIN P53; THIOL DERIVATIVE;

ANIMAL; ARTICLE; BINDING SITE; CELL LINE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON SPIN RESONANCE; GENETICS; MOUSE; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; SPIN LABELING;

ANIMALS; ANTINEOPLASTIC AGENTS; AZURIN; BINDING SITES; CELL LINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN INTERACTION DOMAINS AND MOTIFS; SPIN LABELS; SULFHYDRYL COMPOUNDS; TUMOR SUPPRESSOR PROTEIN P53;

EID: 77958453575     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-010-4069-2     Document Type: Article

References (38)

1. Fialho A M, Stevens F J, Das Gupta T K, et al. Beyond host-pathogen interactions: microbial defense strategy in the host environment. Curr Opin Biotechnol, 2007, 18: 279-286.
2. Yamada T, Goto M, Punj V, et al. The bacterial redox protein azurin induces apoptosis in J774 macrophages through complex formation and stabilization of the tumor suppressor protein p53. Infect Immun, 2002, 70: 7054-7062.
3. Yamada T, Goto M, Punj V, et al. Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer. Proc Natl Acad Sci USA, 2002, 99: 14098-14103.
4. Punj V, Bhattacharyya S, Saint-Dic D, et al. Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer. Oncogene, 2004, 23: 2367-2378.
5. Nar H, Messerschmidt A, van de Kampa R H, et al. Crystal structure of Pseudomonas aeruginosa apo-azurin at 1. 85 Å resolution. FEBS Lett, 1992, 306: 119-124.
6. Nar H, Messerschmidt A, van de Kamp R H, et al. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5. 5 and pH 9. 0. J Mol Biol, 1991, 221: 765-772.
7. Adman E T, Stenkamp R E, Sieker L C, et al. A crystallographic model for azurin at 3 Å resolution. J Mol Biol, 1978, 123: 35-47.
8. Nar H, Huber R, Messerschmidt A, et al. Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin. Eur J Biochem, 1992, 205: 1123-1129.
9. Bonander N, Karlsson BG, Vanngard T. Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa. Biochim Biophys Acta, 1995, 1251: 48-54.
10. Milardi D, Grasso D M, Verbeet M Ph, et al. Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions. Arch Biochem Biophys, 2003, 414: 121-127.
11. van P G, Cigna G, Rolli G, et al. Electron-transfer properties of Pseudomonas aeruginosa Lys44, Glu64 azurin. Eur J Biochem, 1997, 247: 322-331.
12. Yamada T, Fialho A M, Punj V, et al. Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity. Cell Microbiol, 2005, 7: 1418-1431.
13. Taylor B N, Mehta R R, Yamada T, et al. Noncationic peptides obtained from azurin preferentially enter cancer cells. Cancer Res, 2009, 69: 537-46.
14. Yee K S, Vousden K H. Complicating the complexity of p53. Carcinogenesis, 2005, 26: 1317-1322.
15. Vousden K H, Lu X. Live or let die: the cell's response to p53. Nat Rev Cancer, 2002, 2: 594-604.
16. Ryan K M, Phillips A C, Vousden K H. Regulation and function of the p53 tumor suppressor protein. Curr Opin Cell Biol, 2001, 13: 332-337.
17. Hofseth L J, Hussain S P, Harris C C. p53: 25 years after its discovery. Trends Pharmacol Sci, 2004, 25: 177-181.
18. Goto M, Yamada T, Kimbara K, et al. 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, 2003, 47: 549-559.
19. Punj V, Das Gupta T K, Chakrabarty A M. Bacterial cupredoxin azurin and its interactions with the tumor suppressor protein p53. Biochem Biophys Res Commun, 2003, 312: 109-114.
20. Apiyo D, Wittung S P. Unique complex between bacterial azurin and tumor suppressor protein p53. Biochem Biophys Res Commun, 2005, 332: 965-968.
21. Yamada T, Hiraoka Y, Ikehata M, et al. Apoptosis or growth arrest: Modulation of tumor suppressor p53's specificity by bacterial redox protein azurin. Proc Natl Acad Sci USA, 2004, 101: 4770-4775.
22. Hubbell W L, Cafiso D S, Altenbach C. Identifying conformational changes with site-directed spin labeling. Nat Struct Mol Biol, 2000, 7: 735-739.
23. Fanucci G E, Cafiso D S. Recent advances and applications of site-directed spin labeling. Curr Opin Struct Biol, 2006, 16: 644-653.
24. Hubbell W L, Gross A, Langen R, et al. Recent advances in site-directed spin labeling of proteins. Curr Opin Struct Biol, 1998, 8: 649-656.
25. Colunbus L, Hubbell W L. A new spin on protein dynamics. Trends Biochem Sci, 2002, 27: 288-295.
26. Hustedt E J, Beth A H. Nitroxide spin-spin interactions: applications to protein structure and dynamics. Annu Rev Biophys Biomol Struct, 1999, 28: 129-153.
27. van de Kamp M, Hali F C, Rosato N, et al. Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of Pseudomonas aeruginosa azu gene in Escherichia coli. Biochim Biophys Acta, 1990, 1019: 283-292.
28. Bullock A N, Henckel J, DeDecker B S, et al. Thermodynamic stability of wild-type and mutant p53 core domain. Proc Natl Acad Sci USA, 1997, 94: 14338-14342.
29. Bulaj G, Kortemme T, Goldenberg D P. Ionization-reactivity rela tionships for cysteine thiols in polypeptides. Biochemistry, 1998, 37: 8965-8972.
30. Dunham T D, Farrens D L. Conformational changes in rhodopsin: movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy. J Biol Chem, 1999, 274: 1683-1690.
31. Crane J M, Mao C, Lilly A A, et al. Mapping of the docking of Sec A onto the chaperone Sec B by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. J Mol Biol, 2005, 353: 295-307.
32. Berliner L J. Spin Labeling: Theory and Applications. 2nd ed. New York: Academic Press, 1979.
33. Lai C S, Froncisz W, Hopwood L E. An evaluation of paramagnetic broadening agents for spin probe studies of intact mammalian cells. Biophys J, 1987, 52: 625-628.
34. Zhao B L, Li X J, He R G, et al. ESR studies on oxygen consumption during the respiratory burst of human polymorphonuclear leukocytes. Cell Biol Int, 1989, 13: 317-323.
35. Rizzuti B, Sportelli L, Guzzi R. Evidence of reduced flexibility in disulfide bridge-depleted azurin: a molecular dynamics simulation study. Biophys Chem, 2001, 94: 107-120.
36. Miller R. Simultaneous Statistical Inference. New York: Springer, 1981.
37. Taranta M, Bizzarri A R, Cannistraro S. Probing the interaction between p53 and the bacterial protein azurin by single-molecule force spectroscopy. J Mol Recognit, 2008, 21: 63-70.
38. De Grandis V, Bizzarri A R, Cannistraro S. Docking study and free energy simulation of the complex between DNA-binding domain and azurin. J Mol Recognit, 2007, 20: 215-226.