545
Views
29
CrossRef citations to date
0
Altmetric
Commentary & View

The effects of amino acid composition on yeast prion formation and prion domain interactions

&
Pages 60-65 | Received 14 Jan 2010, Accepted 28 Apr 2010, Published online: 01 Apr 2010

References

  • Toombs JA, McCarty BR, Ross ED. Compositional determinants of prion formation in yeast. Mol Cell Biol 2010; 30:319 - 332
  • Ross CD, McCarty BM, Hamilton M, Ben-Hur A, Ross ED. A promiscuous prion: Efficient induction of [URE3] prion formation by heterologous prion domains. Genetics 2009; 183:929 - 940
  • Wickner RB, Shewmaker F, Kryndushkin D, Edskes HK. Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures. Bioessays 2008; 30:955 - 964
  • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146 - 158
  • Du Z, Park KW, Yu H, Fan Q, Li L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 2008; 40:460 - 465
  • Nemecek J, Nakayashiki T, Wickner RB. A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc Natl Acad Sci USA 2009; 106:1892 - 1896
  • Patel BK, Gavin-Smyth J, Liebman SW. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 2009; 11:344 - 349
  • Michelitsch MD, Weissman JS. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 2000; 97:11910 - 11915
  • Ross ED, Baxa U, Wickner RB. Scrambled prion domains form prions and amyloid. Mol Cell Biol 2004; 24:7206 - 7213
  • Ross ED, Edskes HK, Terry MJ, Wickner RB. Primary sequence independence for prion formation. Proc Natl Acad Sci USA 2005; 102:12825 - 12830
  • Harrison PM, Gerstein M. A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol 2003; 4:40
  • DePace AH, Santoso A, Hillner P, Weissman JS. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 1998; 93:1241 - 1252
  • Shewmaker F, Ross ED, Tycko R, Wickner RB. Amyloids of shuffled prion domains that form prions have a parallel in-register beta-sheet structure. Biochemistry 2008; 47:4000 - 4007
  • Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer’s beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Nat Acad Sci USA 2002; 99:16742 - 16747
  • Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 1994; 91:5355 - 5358
  • Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, et al. Structure of the cross-beta spine of amyloid-like fibrils. Nature 2005; 435:773 - 778
  • Alexandrov IM, Vishnevskaya AB, Ter-Avanesyan MD, Kushnirov VV. Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation. J Biol Chem 2008; 283:15185 - 15192
  • Ohhashi Y, Ito K, Toyama BH, Weissman JS, Tanaka M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nature 2010; 6:225 - 230 Epub 2010.
  • Scheibel T, Lindquist SL. The role of conformational flexibility in prion propagation and maintenance for Sup35p. Nat Struct Biol 2001; 8:958 - 962
  • Prilusky J, Felder CE, Zeev-Ben-Mordehai T, Rydberg EH, Man O, Beckmann JS, et al. FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 2005; 21:3435 - 3438
  • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982; 157:105 - 132
  • Esteras-Chopo A, Serrano L, de la Paz ML. The amyloid stretch hypothesis: Recruiting proteins toward the dark side. Proc Natl Acad Sci USA 2005; 102:16672 - 16677
  • Linding R, Schymkowitz J, Rousseau F, Diella F, Serrano L. A comparative study of the relationship between protein structure and [beta]-aggregation in globular and intrinsically disordered proteins. J Mol Biol 2004; 342:345 - 353
  • Osherovich LZ, Cox BS, Tuite MF, Weissman JS. Dissection and design of yeast prions. PLoS Biol 2004; 2:86
  • Santoso A, Chien P, Osherovich LZ, Weissman JS. Molecular basis of a yeast prion species barrier. Cell 2000; 100:277 - 288
  • Liu JJ, Sondheimer N, Lindquist SL. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proc Natl Acad Sci USA 2002; 99:16446 - 16453
  • West MW, Wang W, Patterson J, Mancias JD, Beasley JR, Hecht MH. De novo amyloid proteins from designed combinatorial libraries. Proc Natl Acad Sci USA 1999; 96:11211 - 11216
  • Derkatch IL, Bradley ME, Masse SV, Zadorsky SP, Polozkov GV, Inge-Vechtomov SG, et al. Dependence and independence of [PSI(+)] and [PIN(+)]: a twoprion system in yeast?. EMBO J 2000; 19:1942 - 1952
  • Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. Effects of Q/N-rich, polyQ and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci USA 2004; 101:12934 - 12939
  • Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell 2001; 106:183 - 194
  • Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001; 106:171 - 182
  • Bradley ME, Edskes HK, Hong JY, Wickner RB, Liebman SW. Interactions among prions and prion “strains” in yeast. Proc Natl Acad Sci USA 2002; 99:16392 - 16399
  • Schwimmer C, Masison DC. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol Cell Biol 2002; 22:3590 - 3598
  • Hansen JC, Lu X, Ross ED, Woody RW. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem 2006; 281:1853 - 1856

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.