Microbial specialization by prions

References

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science. 1982;216:136–144.
   PubMed Web of Science ®Google Scholar
• Si K, Giustetto M, Etkin A, et al. A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia. Cell. 2003;115:893–904.
   PubMed Web of Science ®Google Scholar
• Majumdar A, Cesario WC, White-Grindley E, et al. Critical role of amyloid-like oligomers of drosophila Orb2 in the persistence of memory. Cell. 2012;148:515–529.
   PubMed Web of Science ®Google Scholar
• Hou F, Sun L, Zheng H, et al. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell. 2011;146:448–461.
   PubMed Web of Science ®Google Scholar
• Cai X, Chen J, Xu H, et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell. 2014;156:1207–1222.
   PubMed Web of Science ®Google Scholar
• Chakrabortee S, Kayatekin C, Newby GA, et al. Luminidependens (LD) is an Arabidopsis protein with prion behavior. PNAS. 2016;113:6065–6070.
   PubMed Web of Science ®Google Scholar
• Yuan AH, Hochschild A. A bacterial global regulator forms a prion. Science. 2017;355:198–201.
   PubMed Web of Science ®Google Scholar
• Liebman SW, Chernoff YO. Prions in yeast. Genetics. 2012;191:1041–1072.
   PubMed Web of Science ®Google Scholar
• True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature. 2000;407:477–483.
   PubMed Web of Science ®Google Scholar
• Halfmann R, Jarosz DF, Jones SK, et al. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature. 2012;482:363–368.
   PubMed Web of Science ®Google Scholar
• Jarosz DF, Lancaster AK, Brown JCS, et al. An evolutionarily conserved prion-like element converts wild fungi from metabolic specialists to generalists. Cell. 2014;158:1072–1082.
   PubMed Web of Science ®Google Scholar
• Chakrabortee S, Byers JS, Jones S, et al. Intrinsically disordered proteins drive emergence and inheritance of biological traits. Cell. 2016;167:369–381.e12.
   PubMed Web of Science ®Google Scholar
• Cox BS, Tuite MF, Mundy CJ. Reversion from suppression to nonsuppression in SUQ5 [psi+] strains of yeast: the classificaion of mutations. Genetics. 1980;95:589–609.
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Lindquist SL, Ono B, et al. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science. 1995;268:880–884.
   PubMed Web of Science ®Google Scholar
• Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 1994;264:566–569.
   PubMed Web of Science ®Google Scholar
• Sondheimer N, Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell. 2000;5:163–172.
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, et al. Prions affect the appearance of other prions: the story of [PIN+]. Cell. 2001;106:171–182.
   PubMed Web of Science ®Google Scholar
• Michelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. PNAS. 2000;97:11910–11915.
   PubMed Web of Science ®Google Scholar
• Alberti S, Halfmann R, King O, et al. Identifies prions and illuminates sequence features of prionogenic proteins. Cell. 2009;137:146–158.
   PubMed Web of Science ®Google Scholar
• Franzmann TM, Jahnel M, Pozniakovsky A, et al. Phase separation of a yeast prion protein promotes cellular fitness. Science. 2018;359:eaao5654.
   PubMed Web of Science ®Google Scholar
• Han TW, Kato M, Xie S, et al. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. PubMed - NCBI. Cell. 2012;149:768–779.
   Google Scholar
• Kato M, Han TW, Xie S, et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell. 2012;149:753–767.
   PubMed Web of Science ®Google Scholar
• Newby GA, Kiriakov S, Hallacli E, et al. A genetic tool to track protein aggregates and control prion inheritance. Cell [Internet]. 2017;171:966–979.e18.
   Google Scholar
• Du Z, Park K-W, Yu H, et al. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet. 2008;40:460–465.
   PubMed Web of Science ®Google Scholar
• Du Z, Crow ET, Kang HS, et al. Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function. Mol Cell Biol. 2010;30:4644–4655.
   PubMed Web of Science ®Google Scholar
• Hines JK, Li X, Du Z, et al. [SWI+], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity. PLoS Genet. 2011;7:e1001309.
   PubMed Web of Science ®Google Scholar
• Du Z, Goncharoff DK, Cheng X, et al. Analysis of [SWI+] formation and propagation events. Mol Microbiol. 2017;104:105–124.
   PubMed Web of Science ®Google Scholar
• Stern M, Jensen R, Herskowitz I. Five SWI genes are required for expression of the HO gene in yeast. J Mol Biol. 1984;178:853–868.
   PubMed Web of Science ®Google Scholar
• Du Z, Zhang Y, Li L. The yeast prion [SWI+] abolishes multicellular growth by triggering conformational changes of multiple regulators required for flocculin gene expression. Cell Rep. 2015;13:2865–2878.
   PubMed Web of Science ®Google Scholar
• Newby GA, Lindquist S. Pioneer cells established by the [SWI+] prion can promote dispersal and out-crossing in yeast. PLoS Biol. 2017;15:e2003476.
   PubMed Web of Science ®Google Scholar
• Nasmyth K. The determination of mother cell-specific mating type switching in yeast by a specific regulator of HO transcription. EMBO J. 1987;6:243–248.
   PubMed Web of Science ®Google Scholar
• Holmes DL, Lancaster AK, Lindquist S, et al. Heritable remodeling of yeast multicellularity by an environmentally responsive prion. Cell. 2013;153:153–165.
   PubMed Web of Science ®Google Scholar
• Brown JCS, Lindquist S. A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes Dev. 2009;23:2320–2332.
   PubMed Web of Science ®Google Scholar
• Garcia DM, Dietrich D, Clardy J, et al. A common bacterial metabolite elicits prion-based bypass of glucose repression. eLife Sci. 2016;5:76.
   Web of Science ®Google Scholar
• Newby GA, Lindquist S. Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol. 2013;23:251–259.
   PubMed Web of Science ®Google Scholar
• Coustou V, Deleu C, Saupe S, et al. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. PNAS. 1997;94:9773–9778.
   PubMed Web of Science ®Google Scholar
• Yuan AH, Garrity SJ, Nako E, et al. Prion propagation can occur in a prokaryote and requires the ClpB chaperone. eLife Sci. 2014;3:327.
   Web of Science ®Google Scholar
• Khan T, Kandola T, Wu J, et al. Quantifying nucleation in vivo reveals the physical basis of prion-like phase behavior. bioRxiv. 2018;205690.
   Google Scholar