Structural characterization of microcin E492 amyloid formation: Identification of the precursors

Journal of Structural Biology

Volumn 178, Issue 1, 2012, Pages 54-60

  Arranz, Rocío ^a   Mercado, Gabriela ^b   Martín Benito, Jaime ^a   Giraldo, Rafael ^c   Monasterio, Octavio ^b   Lagos, Rosalba ^b   Valpuesta, José M ^a  

^a CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^b UNIVERSITY OF CHILE   (Chile)

^c CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

Author keywords

Amyloid; Electron microscopy; Image processing; Microcin

Indexed keywords

AMYLOID; BACTERIAL TOXIN; MICROCIN E492; UNCLASSIFIED DRUG;

ARTICLE; ELECTRON MICROSCOPY; FIBER; IMAGE PROCESSING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; TOXIN STRUCTURE; X RAY DIFFRACTION;

AMYLOID; BACTERIOCINS; KLEBSIELLA PNEUMONIAE; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; X-RAY DIFFRACTION;

EID: 84859419339     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.02.015     Document Type: Article

References (28)

1. Berstein S.L., Dupuis N.F., Lazo N.D., Wyttenbach T., Condron M.M., et al. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 2009, 1:326-331.
2. Bian W., Wang H., McCullough I., Stubbs G. WCEN: a computer program for initial processing of fiber diffraction patterns. J. Appl. Cryst. 2006, 39:752-756.
3. Bieler S., Estrada L., Lagos R., Baeza M., Castilla J., et al. Amyloid formation modulates the biological activity of a bacterial protein. J. Biol. Chem. 2005, 280:26880-26885.
4. Caughey B., Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 2003, 26:267-298.
5. Chapman M.R., Robinson L.S., Pinkner J.S., Roth R., Heuser J., et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 2002, 295:851-855.
6. Corsini G., Baeza M., Monasterio O., Lagos R. The expression of genes involved in microcin maturation regulates the production of active microcin E492. Biochimie 2002, 84:539-544.
7. de Lorenzo V. Isolation and characterization of microcin E492 from Klebsiella pneumoniae. Arch. Microbiol. 1984, 139:72-75.
8. de Lorenzo V., Pugsley A.P. Microcin E492, a low-molecular-weight peptide antibiotic which causes depolarization of the Escherichia coli cytoplasmic membrane. Antimicrob. Agents Chemother. 1985, 27:666-669.
9. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24:329-332.
10. Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
11. Fischer H., Polikarpov I., Craievich A.F. Average protein density is a molecular-weight-dependent function. Protein Sci. 2004, 13:2825-2828.
12. Hetz C., Bono M.R., Barros L.F., Lagos R. Microcin E492, a channel-forming bacteriocin from Klebsiella pneumoniae, induces apoptosis in some human cell lines. Proc. Natl. Acad. Sci. USA 2002, 99:2696-2701.
13. Kayed R., Sokolov Y., Edmonds B., McIntire T.M., Milton S.C., et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 2004, 279:46363-46366.
14. Lagos R., Wilkens M., Vergara C., Cecchi X., Monasterio O. Microcin E492 forms ion channels in phospholipid bilayer membrane. FEBS Lett. 1993, 321:145-148.
15. Lagos R., Baeza M., Corsini G., Hetz C., Strahsburger E., et al. Structure, organization, and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin. Mol. Microbiol. 2001, 42:229-243.
16. Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002, 418:291.
17. Lashuel H.A., Petre B., Wall J., Simon M., Nowak R., et al. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 2002, 322:1089-1102.
18. Lashuel H.A., Lansbury P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?. Q. Rev. Biophys. 2006, 39:167-201.
19. Mercado G., Tello M., Marín M., Monasterio O., Lagos R. The production in vivo of microcin E492 with antibacterial activity depends on salmochelin and EntF. J. Bacteriol. 2008, 190:5464-5471.
20. Miller J.H. Experiments in Molecular Genetics 1972, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp. 431-435.
21. Nelson R., Eisenberg D. Structural models of amyloid-like fibrils. Adv. Protein Chem. 2006, 73:235-282.
22. Orellana C., Lagos R. The activity of microcin E492 from Klebsiella pneumoniae is regulated by a microcin antagonist. FEMS Microbiol. Lett. 1996, 136:297-303.
23. Quist A., Doudevski I., Lin H., Azimova R., Ng D., et al. Amyloid ion channels: a common structural link for protein-misfolding disease. Proc. Natl. Acad. Sci. USA 2005, 102:10427-10432.
24. Roychaudhuri R., Yang M., Hoschi M.M., Teplow D.B. Amyloid β-protein assembly and Alzheimer disease. J. Biol. Chem. 2009, 284:4749-4753.
25. Sachse C., Fändrich M., Grigorieff N. Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy. Proc. Natl. Acad. Sci. USA 2008, 105:7462-7466.
26. Scheres S.H.W., Valle M., Núñez R., Sorzano C.O.S., Marabini R., et al. Maximum-likelihood multi-reference refinement for electron microscopy images. J. Mol. Biol. 2005, 348:139-149.
27. Sorzano C.O.S., Marabini R., Velázquez-Muriel J., Bilbao-Castro J.R., Scheres S.H.W., et al. XMIPP: a new generation of an open-source image processing package for electron microscopy. J. Struct. Biol. 2004, 148:194-204.
28. Soscia S.J., Kirby J.E., Washicosky K.J., Tucker S.M., Ingelsson M., et al. The Alzheimer's disease-associated amyloid β-protein is an antimicrobial peptide. PLoS One 2010, 5:e9505. 10.1371/journal.pone.0009505.