#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Yeast Prions: Proteins Templating Conformation and an Anti-prion System


article has not abstract


Vyšlo v časopise: Yeast Prions: Proteins Templating Conformation and an Anti-prion System. PLoS Pathog 11(2): e32767. doi:10.1371/journal.ppat.1004584
Kategorie: Pearls
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004584

Souhrn

article has not abstract


Zdroje

1. Wickner RB (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in S. cerevisiae. Science 264: 566–569. 7909170

2. King CY, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428: 319–323. 15029195

3. Tanaka M, Chien P, Naber N, Cooke R, Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323–328. 15029196

4. Brachmann A, Baxa U, Wickner RB (2005) Prion generation in vitro: amyloid of Ure2p is infectious. Embo J 24: 3082–3092. 16096644

5. Liebman SW, Chernoff YO (2012) Prions in yeast. Genetics 191: 1041–1072. doi: 10.1534/genetics.111.137760 22879407

6. Wickner RB, Edskes HK, Bateman DA, Kelly AC, Gorkovskiy A, et al. (2013) Amyloids and yeast prion biology. Biochemistry 52: 1514–1527. doi: 10.1021/bi301686a 23379365

7. Saupe SJ (2011) The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility. Sem Cell & Dev Biol 22: 460–468. doi: 10.1016/j.semcdb.2011.02.019 21334447

8. Kraus A, Groveman BR, Caughey B (2013) Prions and the potential transmissibility of protein misfolding diseases. Ann Rev Microbiol 67: 543–564. doi: 10.1146/annurev-micro-092412-155735 23808331

9. Derkatch IL, Chernoff YO, Kushnirov VV, Inge-Vechtomov SG, Liebman SW (1996) Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144: 1375–1386. 8978027

10. King CY (2001) Supporting the structural basis of prion strains: induction and identification of [PSI] variants. J Mol Biol 307: 1247–1260. 11292339

11. McGlinchey R, Kryndushkin D, Wickner RB (2011) Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci USA 108: 5337–5341. doi: 10.1073/pnas.1102762108 21402947

12. Nakayashiki T, Kurtzman CP, Edskes HK, Wickner RB (2005) Yeast prions [URE3] and [PSI+] are diseases. Proc Natl Acad Sci U S A 102: 10575–10580. 16024723

13. Halfmann R, Jarosz DF, Jones SK, Chang A, Lancster AK, et al. (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482: 363–368. doi: 10.1038/nature10875 22337056

14. Edskes HE, Khamar HJ, Winchester C-L, Greenler AJ, Zhou A, et al. (2014) Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi. Genetics epub ahead of print.

15. Shewmaker F, Wickner RB, Tycko R (2006) Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure. Proc Natl Acad Sci USA 103: 19754–19759. 17170131

16. Gorkovskiy A, Thurber KR, Tycko R, Wickner RB (2014) Locating the folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid. Proc Natl Acad Sci USA 111: in press. doi: 10.1073/pnas.1421566112 25552562

17. Collins SR, Douglass A, Vale RD, Weissman JS (2004) Mechanism of prion propagation: amyloid growth occurs by monomer addition. Plos Biol 2: 1582–1590.

18. Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T (2007) Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 5: 611–618. 17632572

19. Kryndushkin D, Shewmaker F, Wickner RB (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27: 2725–2735. doi: 10.1038/emboj.2008.198 18833194

20. Edskes HK, Gray VT, Wickner RB (1999) The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci USA 96: 1498–1503. 9990052

21. Wickner RB, Beszonov E, Bateman DA (2014) Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants. Proc Natl Acad Sci USA. doi: 10.1073/pnas.1421566112 25552562

22. Wang Y, Meriin AB, Zaarur N, Romanova NV, Chernoff YO, et al. (2009) Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 23: 451–463. doi: 10.1096/fj.08-117614 18854435

23. Gardner RG, Nelson ZW, Gottschling DE (2005) Degradation-mediated protein quality control in the nucleus. Cell 120: 803–815. 15797381

24. Specht S, Miller SBM, Mogk A, Bukau B (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 195: 617–629. doi: 10.1083/jcb.201106037 22065637

25. Malinovska L, Kroschwald S, Munder MC, Richter D, Alberti S (2012) Molecular chaperones and stress-inducible protein-sorting factors coordinate the spaciotemporal distribution of protein aggregates. Mol Biol Cell 23: 3041–3056. doi: 10.1091/mbc.E12-03-0194 22718905

26. Kryndushkin D, Ihrke G, Piermartiri TC, Shewmaker F (2012) A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity. Mol Microbiol Epub ahead of print.

27. Bessen RA, Marsh RF (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66: 2096–2101. 1347795

28. Liebman SW, Chernoff YO (2012) Prions in yeast. Genetics 191: 1041–1072. doi: 10.1534/genetics.111.137760 22879407

Štítky
Hygiena a epidemiológia Infekčné lekárstvo Laboratórium

Článok vyšiel v časopise

PLOS Pathogens


2015 Číslo 2
Najčítanejšie tento týždeň
Najčítanejšie v tomto čísle
Kurzy

Zvýšte si kvalifikáciu online z pohodlia domova

Aktuální možnosti diagnostiky a léčby litiáz
nový kurz
Autori: MUDr. Tomáš Ürge, PhD.

Všetky kurzy
Prihlásenie
Zabudnuté heslo

Zadajte e-mailovú adresu, s ktorou ste vytvárali účet. Budú Vám na ňu zasielané informácie k nastaveniu nového hesla.

Prihlásenie

Nemáte účet?  Registrujte sa

#ADS_BOTTOM_SCRIPTS#