Microbial Prions: Dawn of a New Era

Levkovich, Shon A.; Rencus‐Lazar, Sigal; Gazit, Ehud; Bar-Yosef, Dana Laor

doi:10.1016/j.tibs.2020.12.006

Cited by 13 publications

(13 citation statements)

References 93 publications

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“…By definition, canonical prions exhibit QN-rich domains but also the ability to populate amyloid supramolecular conformations and a Hsp104-dependent cell-to-cell propagation [72,73]. Although it is not the scope of this review, it is worth to mention that certain proteins lacking these canonical traits may act as prions, including the so-called mnemons, which can suffer conformational switches, but cannot propagate to daughter cells, acting as a kind of cellular memory [74,75].…”

Section: Proteome-wide Analysis Of Prion-like Proteins In Different Kingdoms Of Lifementioning

confidence: 99%

Prion‐like proteins: from computational approaches to proteome‐wide analysis

et al. 2021

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Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations.The notion that such proteins could play functional roles and be positively selected by evolution has triggered the development of computational tools to identify prion-like proteins in different kingdoms of life. These algorithms have succeeded in screening multiple proteomes, allowing the identification of prion-like proteins in a diversity of unrelated organisms, evidencing that the prion phenomenon is well conserved among species. Interestingly enough, prion-like proteins are not only connected with the formation of functional membraneless protein-nucleic acid coacervates, but are also linked to human diseases. This review addresses state-of-the-art computational approaches to identify prion-like proteins, describes proteome-wide analysis efforts, discusses these unique proteins' functional role, and illustrates recently validated examples in different domains of life.

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Section: Proteome-wide Analysis Of Prion-like Proteins In Different Kingdoms Of Lifementioning

confidence: 99%

Prion‐like proteins: from computational approaches to proteome‐wide analysis

et al. 2021

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“…The selection of mechanisms (prions or mnemons) may relate to which strategy would be more efficient. While the adaptive advantages of prions have been discussed, 43 , 44 , 45 mnemons provide an individualized mechanism for single cells to adapt to a signal and keep the opportunity for their progeny to remain naive. The value of such a strategy is evident in the case of mating because the daughter cells might be better placed relative to a potential partner to allow for a successful mating; however, in reverse, the stable propagation of the refractory state has the disadvantage of turning a single deceptive encounter into the sterility of the entire subsequent colony.…”

Section: Discussionmentioning

confidence: 99%

Whi3 mnemon association with endoplasmic reticulum membranes confines the memory of deceptive courtship to the yeast mother cell

et al. 2022

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Whi3 mnemon association with endoplasmic reticulum membranes confines the memory of deceptive courtship to the yeast mother cell Highlights d Whi3 mnemon associates with endoplasmic reticulum membranes d Diffusion barriers restricts Whi3 mnemon inheritance to the mother cell d Whi3 prion-like domain can assemble in self-templating fibrils in vitro d Whi3 can adopt a prion-like behavior in diffusion barrierdefective cells

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“…Perhaps the most important protein that controls propagation of all known amyloid yeast prions is Hsp104, a chaperone that acts as a disaggregase by rescuing previously misfolded and aggregated proteins [46,47] (reviewed in [4]). Hsp104 is strictly required for maintenance of all known amyloid yeast prions (propagation of non-amyloid prions depends on other chaperone groups-Hsp70 (e.g., for [SMAUG + ], [GAR + ]) or Hsp90 (e.g., for [ESI + ]) (reviewed in [48])). Deletion of HSP104, its dominant negative mutation (e.g., Hsp104KT [49,50]) or inhibition with chemical agents such as guanidine hydrochloride (GuHCl) eliminates prions [27,49,51,52] (reviewed in [9]).…”

Section: Hsp104mentioning

confidence: 99%

Differential Interactions of Molecular Chaperones and Yeast Prions

Barbitoff

Matveenko

Zhouravleva

2022

JoF

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Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction between the protein quality control (PQC) machinery and misfolded proteins. More than ten prions have been identified in yeast, of which the most studied ones include [PSI+], [URE3], and [PIN+]. While all of the major molecular chaperones have been implicated in propagation of yeast prions, many of these chaperones differentially impact propagation of different prions and/or prion variants. In this review, we summarize the current understanding of the life cycle of yeast prions and systematically review the effects of different chaperone proteins on their propagation. Our analysis clearly shows that Hsp40 proteins play a central role in prion propagation by determining the fate of prion seeds and other amyloids. Moreover, direct prion-chaperone interaction seems to be critically important for proper recruitment of all PQC components to the aggregate. Recent results also suggest that the cell asymmetry apparatus, cytoskeleton, and cell signaling all contribute to the complex network of prion interaction with the yeast cell.

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Microbial Prions: Dawn of a New Era

Cited by 13 publications

References 93 publications

Prion‐like proteins: from computational approaches to proteome‐wide analysis

Prion‐like proteins: from computational approaches to proteome‐wide analysis

Whi3 mnemon association with endoplasmic reticulum membranes confines the memory of deceptive courtship to the yeast mother cell

Differential Interactions of Molecular Chaperones and Yeast Prions

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