Yeast and Fungal Prions

Wickner, Reed B.

doi:10.1101/cshperspect.a023531

Cited by 73 publications

(41 citation statements)

References 140 publications

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“…eRF3 is composed of an N-terminal regulatory region and a Cterminal GTPase catalytic region (eRF3c), which is essential for translation termination. The eRF3 Nterminal region interacts with various factors [41,42], and contains unique motif sequences that can induce a [PSI+] prion-like phenotypes [43]. Unlike eukaryotes, in prokaryotes, class I release factors, RF1 and RF2, decipher UAG/UAA and UGA/UAA codons respectively [32,44].…”

mentioning

confidence: 99%

Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae

Wada

Ito

2018

The FEBS Journal

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The CGA arginine codon is a rare codon in Saccharomyces cerevisiae. Thus, full‐length mature protein synthesis from reporter genes with internal CGA codon repeats are markedly reduced, and the reporters, instead, produce short‐sized polypeptides via an unknown mechanism. Considering the product size and similar properties between CGA sense and UGA stop codons, we hypothesized that eukaryote polypeptide‐chain release factor complex eRF1/eRF3 catalyses polypeptide release at CGA repeats. Herein, we performed a series of analyses and report that the CGA codon can be, to a certain extent, decoded as a stop codon in yeast. This also raises an intriguing possibility that translation termination factors eRF1/eRF3 rescue ribosomes stalled at CGA codons, releasing premature polypeptides, and competing with canonical tRNAICG to the CGA codon. Our results suggest an alternative ribosomal rescue pathway in eukaryotes. The present results suggest that misdecoding of low efficient codons may play a novel role in global translation regulation in S. cerevisiae.

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confidence: 99%

Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae

Wada

Ito

2018

The FEBS Journal

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“…Much of our molecular understanding of prions originates from studies in yeast, where over ten bona fide prion proteins have been characterized to date (Table 1) [60,73,82]. Unlike mammalian PrP, certain prions in yeast have been proposed to play useful regulatory functions (see below).…”

Section: Heritable Assemblies: Prionsmentioning

confidence: 99%

Protein assembly systems in natural and synthetic biology

2020

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The traditional view of protein aggregation as being strictly disease-related has been challenged by many examples of cellular aggregates that regulate beneficial biological functions. When coupled with the emerging view that many regulatory proteins undergo phase separation to form dynamic cellular compartments, it has become clear that supramolecular assembly plays wide-ranging and critical roles in cellular regulation. This presents opportunities to develop new tools to probe and illuminate this biology, and to harness the unique properties of these selfassembling systems for synthetic biology for the purposeful manipulation of biological function.

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“…Prion strains or variants are distinct infectious conformations of the same prion protein (Colby and Prusiner, ; Wickner, ). An infectious conformation propagates by converting the cellular protein to its like, thereby generating new infectivity.…”

Section: Introductionmentioning

confidence: 99%

Forms and abundance of chaperone proteins influence yeast prion variant competition

King

2019

Molecular Microbiology

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Summary [PSI+] variants are different infectious conformations of the same Sup35 protein. We show that when [PSI+] variants VK and VL co‐infect a dividing host, only one prevails in the end and the host genetic background is involved in winner selection. In the 5V‐H19 background, the VK variant dominates over the VL variant. The order of dominance is reversed in the 74‐D694 background, where VL can coexists with VK for a short period, but will eventually take over. Differential interaction of chaperone proteins with distinct prion variant conformations can influence the outcome of competition. Expanding the Glycine/Methionine‐rich domain of Sis1, an Hsp40 protein, helps the propagation of VL. Over‐expression of the Hsp70 protein Ssa2 lowers the number of prion particles (propagons) in the cell. There is more reduction for VK than VL, causing the latter to dominate in some of the 5V‐H19 and all of the 74‐D694 cells tested. Consistently, depleting Ssa1 in 74‐D694 strengthens VK. Swapping chromosomal alleles of SSA1/2 and SIS1 between 5V‐H19 and 74‐D694, including cognate promoters, is not sufficient to change the native dominance order of each background, suggesting there exist additional polymorphic factors that modulate [PSI+] competition.

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Yeast and Fungal Prions

Cited by 73 publications

References 140 publications

Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae

Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae

Protein assembly systems in natural and synthetic biology

Forms and abundance of chaperone proteins influence yeast prion variant competition

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