Access the full text.
Sign up today, get DeepDyve free for 14 days.
R Ramanagoudr-Bhojappa, LP Blair, AJ Tackett, KD Raney (2013)
Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding proteinNucleic Acids Res, 41
J Saarikangas, Y Barral (2016)
Protein aggregation as a mechanism of adaptive cellular responsesCurr Genet, 62
AC Tsolis, NC Papandreou, VA Iconomidou, SJ Hamodrakas (2013)
A consensus method for the prediction of “aggregation-prone” peptides in globular proteinsPLoS One, 8
D Kryndushkin, N Pripuzova, B Burnett, F Shewmaker (2013)
Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cellsJ Biol Chem, 288
RJ Burgess, MP Guy, Z Zhang (2009)
Fueling transcriptional silencing with Gas1Proc Natl Acad Sci USA, 106
M Humenik, AM Smith, S Arndt, T Scheibel (2015)
Ion and seed dependent fibril assembly of a spidroin core domainJ Struct Biol, 191
AA Nizhnikov, TA Ryzhova, KV Volkov, SP Zadorsky, JV Sopova, SG Inge-Vechtomov, AP Galkin (2016)
Interaction of prions causes heritable traits in Saccharomyces cerevisiaePLoS Genet, 12
JR Broach, JN Strathern, JB Hicks (1979)
Transformation in yeast: development of a hybrid cloning vector and isolation of the can1 geneGene, 8
VN Urakov, AB Vishnevskaya, IM Alexandrov, VV Kushnirov, VN Smirnov, MD Ter-Avanesyan (2010)
Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functionsPrion, 4
MR Koch, L Pillus (2009)
The glucanosyltransferase Gas1 functions in transcriptional silencingProc Natl Acad Sci USA, 106
VV Kushnirov, MD Ter-Avanesyan (1998)
Structure and replication of yeast prionsCell, 94
MR Chapman, LS Robinson, JS Pinkner, R Roth, J Heuser, M Hammar, S Normark, SJ Hultgren (2002)
Role of Escherichia coli curli operons in directing amyloid fiber formationScience, 295
JM Kenney, D Knight, MJ Wise, F Vollrath (2002)
Amyloidogenic nature of spider silkEur J Biochem, 269
SB Prusiner (1982)
Novel proteinaceous infections particles cause scrapieScience, 216
YO Chernoff, DA Kiktev (2016)
Dual role of ribosome associated chaperones in prion formation and propagationCurr Genet, 62
J Moreno-García, JC Mauricio, J Moreno, T García-Martínez (2017)
Differential proteome analysis of a flor yeast strain under biofilm formationInt J Mol Sci, 18
PK Teng, D Eisenberg (2009)
Short protein segments can drive a non-fibrillizing protein into the amyloid stateProtein Eng Des Sel, 22
TS Kalebina, TA Plotnikova, AA Gorkovskii, IO Selyakh, OV Galzitskaya (2008)
Amyloid-like properties of Saccharomyces cerevisiae cell wall glucantransferase Bgl2p: prediction and experimental evidencesPrion, 2
K Schwartz, BR Boles (2013)
Microbial amyloids-functions and interactions within the hostCurr Opin Microbiol, 16
E Ragni, T Fontaine, C Gissi, JP Latgè, L Popolo (2007)
The Gas family of proteins of Saccharomyces cerevisiae: characterization and evolutionary analysisYeast, 24
K Si, S Lindquist, ER Kandel (2003)
A neuronal isoform of the aplysia CPEB has prion-like propertiesCell, 115
SN Bagriantsev, VV Kushnirov, SW Liebman (2006)
Analysis of amyloid aggregates using agarose gel electrophoresisMethods Enzymol, 412
AA Nizhnikov, AI Alexandrov, TA Ryzhova, OV Mitkevich, AA Dergalev, MD Ter-Avanesyan, AP Galkin (2014)
Proteomic screening for amyloid proteinsPLoS One, 9
V Sivanathan, A Hochschild (2012)
Generating extracellular amyloid aggregates using E. coli cellsGenes Dev, 26
DM Fowler, AV Koulov, C Alory-Jost, MS Marks, WE Balch, JW Kelly (2006)
Functional amyloid formation within mammalian tissuePLoS Biol, 4
A Majumdar, WC Cesario, E White-Grindley, H Jiang, F Ren, MR Khan, L Li, EM Choi, K Kannan, F Guo, J Unruh, B Slaughter, K Si (2012)
Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memoryCell, 148
KD Allen, RD Wegrzyn, TA Chernova, S Müller, GP Newnam, PA Winslett, KB Wittich, KD Wilkinson, YO Chernoff (2005)
Hsp70 chaperones as modulators of prion life cycle. Novel effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+]Genetics, 169
DS Kryndushkin, IM Alexandrov, MD Ter-Avanesyan, VV Kushnirov (2003)
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104J Biol Chem, 278
RB Wickner (1994)
[URE3] as an altered Ure2 protein: evidence for a prion analog in Saccharomyces cerevisiaeScience, 264
M Yuga, K Gomi, DJ Klionsky, T Shintani (2011)
Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiaeJ Biol Chem, 286
M Destruelle, H Holzer, DJ Klionsky (1994)
Identification and characterization of a novel yeast gene: the YGP1 gene product is a highly glycosylated secreted protein that is synthesized in response to nutrient limitationMol Cell Biol, 14
LS Robinson, EM Ashman, SJ Hultgren, MR Chapman (2006)
Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG proteinMol Microbiol, 59
I Sarto-Jackson, L Tomaska (2016)
How to bake a brain: yeast as a model neuronCurr Genet, 62
TC Brennan, JO Krömer, LK Nielsen (2013)
Physiological and transcriptional responses of Saccharomyces cerevisiae to d-limonene show changes to the cell wall but not to the plasma membraneAppl Environ Microbiol, 79
YO Chernoff, GP Newnam, J Kumar, K Allen, AD Zink (1999)
Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prionMol Cell Biol, 19
SK Park, JY Hong, F Arslan, V Kanneganti, B Patel, A Tietsort, EMH Tank, X Li, SJ Barmada, SW Liebman (2017)
Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysisPLoS Genet, 13
TA Plotnikova, IO Selyakh, TS Kalebina, IS Kulaev (2006)
Bgl2p and Gas1p are the major glucan transferases forming the molecular ensemble of yeast cell wallDokl Biochem Biophys, 409
JD Sipe, MD Benson, JN Buxbaum, S Ikeda, G Merlini (2012)
Amyloid fibril protein nomenclature: 2012 recommendations from the Nomenclature Committee of the International Society of AmyloidosisAmyloid, 19
V Sivanathan, A Hochschild (2013)
A bacterial export system for generating extracellular amyloid aggregatesNat Protoc, 8
KS Antonets, HM Sargsyan, AA Nizhnikov (2016)
Glutamine/Asparagine-rich fragment of Gln3, but not the full-length protein, aggregates in Saccharomyces cerevisiaeBiochemistry (Mosc), 81
EE Bezsonov, M Groenning, OV Galzitskaya, AA Gorkovskii, GV Semisotnov, IO Selyakh, RH Ziganshin, VV Rekstina, IB Kudryashova, SA Kuznetsov, IS Kulaev, TS Kalebina (2013)
Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formationPrion, 7
GP Newnam, RD Wegrzyn, SL Lindquist, YO Chernoff (1999)
Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curingMol Cell Biol, 19
YO Chernoff (2001)
Mutation processes at the protein level: is Lamarck back?Mutat Res, 488
JP Bardill, JE Dulle, JR Fisher, HL True (2009)
Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionPrion, 3
D Vandenbosch, E Canck, I Dhondt, P Rigole, H Nelis, T Coenye (2013)
Genomewide screening for genes involved in biofilm formation and miconazole susceptibility in Saccharomyces cerevisiaeFEMS Yeast Res, 13
The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative disorders such as Alzheimer’s, Parkinson’s Huntington’s diseases. At the same time, a set of amyloids regulates vital processes in archaea, prokaryotes and eukaryotes. Our knowledge of the prevalence and biological significance of amyloids is limited due to the lack of universal methods for their identification. Here, using our original method of proteomic screening PSIA–LC–MALDI, we identified a number of proteins that form amyloid-like detergent-resistant aggregates in Saccharomyces cerevisiae. We revealed in yeast strains of different origin known yeast prions, prion-associated proteins, and a set of proteins whose amyloid properties were not shown before. A substantial number of the identified proteins are cell wall components, suggesting that amyloids may play important roles in the formation of this extracellular protective sheath. Two proteins identified in our screen, Gas1 and Ygp1, involved in biogenesis of the yeast cell wall, were selected for detailed analysis of amyloid properties. We show that Gas1 and Ygp1 demonstrate amyloid properties both in vivo in yeast cells and using the bacteria-based system C-DAG. Taken together, our data show that this proteomic approach is very useful for identification of novel amyloids.
Current Genetics – Springer Journals
Published: Oct 11, 2017
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.