Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion

Microbial Cell Factories

Volumn 8, Issue , 2009, Pages

  Sabaté, Raimon ^a   Espargaró, Alba ^a   Saupe, Sven J ^b   Ventura, Salvador ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CONGO RED; DNA FRAGMENT; PRION PROTEIN; PRION PROTEIN HET; UNCLASSIFIED DRUG; FUNGAL PROTEIN; HET S PROTEIN, PODOSPORA ANSERINA; HET-S PROTEIN, PODOSPORA ANSERINA; PROTEINASE K;

ARTICLE; BACTERIAL INCLUSION BODY; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; DENATURATION; NONHUMAN; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; CHEMISTRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PRION; PROTEIN TERTIARY STRUCTURE;

BACTERIA (MICROORGANISMS); FUNGAL PRION; HET-S PRION;

AMYLOID; ENDOPEPTIDASE K; FUNGAL PROTEINS; INCLUSION BODIES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PRIONS; PROTEIN STRUCTURE, TERTIARY;

EID: 71149094496     PISSN: None     EISSN: 14752859     Source Type: None    
DOI: 10.1186/1475-2859-8-56     Document Type: Article

References (28)

1. Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75:333-366. 10.1146/annurev.biochem.75.101304.123901, 16756495.
2. Ventura S, Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol 2006, 24(4):179-185. 10.1016/j.tibtech.2006.02.007, 16503059.
3. de Groot NS, Espargaro A, Morell M, Ventura S. Studies on bacterial inclusion bodies. Future Microbiol 2008, 3:423-435. 10.2217/17460913.3.4.423, 18651814.
4. Carrio M, Gonzalez-Montalban N, Vera A, Villaverde A, Ventura S. Amyloid-like properties of bacterial inclusion bodies. J Mol Biol 2005, 347(5):1025-1037. 10.1016/j.jmb.2005.02.030, 15784261.
5. Prusiner SB. Shattuck lecture--neurodegenerative diseases and prions. N Engl J Med 2001, 344(20):1516-1526. 10.1056/NEJM200105173442006, 11357156.
6. Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994, 264(5158):566-569. 10.1126/science.7909170, 7909170.
7. Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 2007, 5(8):611-618. 10.1038/nrmicro1708, 2376760, 17632572.
8. Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci USA 1997, 94(18):9773-9778. 10.1073/pnas.94.18.9773, 23266, 9275200.
9. Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, Forge V, Bathany K, Lascu I, Schmitter JM, Riek R. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. Embo J 2003, 22(9):2071-2081. 10.1093/emboj/cdg213, 156085, 12727874.
10. Ritter C, Maddelein ML, Siemer AB, Luhrs T, Ernst M, Meier BH, Saupe SJ, Riek R. Correlation of structural elements and infectivity of the HET-s prion. Nature 2005, 435(7043):844-848. 10.1038/nature03793, 1567094, 15944710.
11. Balguerie A, Dos Reis S, Coulary-Salin B, Chaignepain S, Sabourin M, Schmitter JM, Saupe SJ. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo. J Cell Sci 2004, 117(Pt 12):2599-2610. 10.1242/jcs.01116, 15159455.
12. Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 2008, 319(5869):1523-1526. 10.1126/science.1151839, 18339938.
13. Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe SJ. Amyloid aggregates of the HET-s prion protein are infectious. Proc Natl Acad Sci USA 2002, 99(11):7402-7407. 10.1073/pnas.072199199, 124243, 12032295.
14. Sabate R, Baxa U, Benkemoun L, Sanchez de Groot N, Coulary-Salin B, Maddelein ML, Malato L, Ventura S, Steven AC, Saupe SJ. Prion and non-prion amyloids of the HET-s prion forming domain. J Mol Biol 2007, 370(4):768-783. 10.1016/j.jmb.2007.05.014, 17532341.
15. Wasmer C, Soragni A, Sabate R, Lange A, Riek R, Meier BH. Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra. Angew Chem Int Ed Engl 2008, 47(31):5839-5841. 10.1002/anie.200704896, 18548467.
16. Wasmer C, Benkemoun L, Sabate R, Steinmetz MO, Coulary-Salin B, Wang L, Riek R, Saupe SJ, Meier BH. Solid-State NMR Spectroscopy Reveals that E. coli Inclusion Bodies of HET-s(218-289) are Amyloids. Angew Chem Int Ed Engl 2009, 48(26):4858-4860. 10.1002/anie.200806100, 19472238.
17. Sabate R, Saupe SJ. Thioflavin T fluorescence anisotropy: an alternative technique for the study of amyloid aggregation. Biochem Biophys Res Commun 2007, 360(1):135-138. 10.1016/j.bbrc.2007.06.063, 17586468.
18. Nyrkova IA, Semenov AN, Aggeli A, Boden N. Fibril stability in solutions of twisted b-sheet peptides: a new kind of micellization in chiral systems. Eur Phys J B 2000, 17:481-497.
19. Dos Reis S, Coulary-Salin B, Forge V, Lascu I, Begueret J, Saupe SJ. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J Biol Chem 2002, 277(8):5703-5706. 10.1074/jbc.M110183200, 11733532.
20. De Groot NS, Sabate R, Ventura S. Amyloids in bacterial incluison bodies. Trends Biochem Sci 2009,
21. Morell M, Bravo R, Espargaro A, Sisquella X, Aviles FX, Fernandez-Busquets X, Ventura S. Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochim Biophys Acta 2008, 1783(10):1815-1825. 10.1016/j.bbamcr.2008.06.007, 18619498.
22. Sen A, Baxa U, Simon MN, Wall JS, Sabate R, Saupe SJ, Steven AC. Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils. J Biol Chem 2007, 282(8):5545-5550. 10.1074/jbc.M611464200, 17178708.
23. Espargaro A, Sabate R, Ventura S. Kinetic and thermodynamic stability of bacterial intracellular aggregates. FEBS Lett 2008, 582(25-26):3669-3679. 10.1016/j.febslet.2008.09.049, 18840434.
24. Jarrett JT, Lansbury PT. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 1993, 73(6):1055-1058. 10.1016/0092-8674(93)90635-4, 8513491.
25. Wasmer C, Schutz A, Loquet A, Buhtz C, Greenwald J, Riek R, Bockmann A, Meier BH. The Molecular Organization of the Fungal Prion HET-s in Its Amyloid Form. J Mol Biol 2009, 394(1):119-127. 10.1016/j.jmb.2009.09.015, 19748509.
26. Chien P, Weissman JS, DePace AH. Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004, 73:617-656. 10.1146/annurev.biochem.72.121801.161837, 15189155.
27. Carrio MM, Cubarsi R, Villaverde A. Fine architecture of bacterial inclusion bodies. FEBS Lett 2000, 471(1):7-11. 10.1016/S0014-5793(00)01357-0, 10760503.
28. Sabate R, Gallardo M, Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 2003, 71(2):190-195. 10.1002/bip.10441, 12767118.