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Tytuł pozycji:

Prion-like proteins as epigenetic devices of stress adaptation.

Tytuł:
Prion-like proteins as epigenetic devices of stress adaptation.
Autorzy:
Oamen HP; School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Lau Y; School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, E1 4NS, UK.
Caudron F; School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, E1 4NS, UK. Electronic address: .
Źródło:
Experimental cell research [Exp Cell Res] 2020 Nov 01; Vol. 396 (1), pp. 112262. Date of Electronic Publication: 2020 Sep 05.
Typ publikacji:
Journal Article; Review
Język:
English
Imprint Name(s):
Publication: Orlando Fl : Academic Press
Original Publication: New York, Academic Press.
MeSH Terms:
Epigenesis, Genetic*
Carrier Proteins/*genetics
Molecular Chaperones/*genetics
Prions/*genetics
RNA-Binding Proteins/*genetics
Saccharomyces cerevisiae/*genetics
Saccharomyces cerevisiae Proteins/*genetics
Transcription Factors/*genetics
Adaptation, Physiological/genetics ; Animals ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; GPI-Linked Proteins/chemistry ; GPI-Linked Proteins/genetics ; GPI-Linked Proteins/metabolism ; Genotype ; Humans ; Molecular Chaperones/metabolism ; Phenotype ; Prions/chemistry ; Prions/metabolism ; Protein Conformation ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Stress, Physiological ; Transcription Factors/chemistry ; Transcription Factors/metabolism
Contributed Indexing:
Keywords: Chaperones; Memory; Mnemon; Prion; Stress
Substance Nomenclature:
0 (Carrier Proteins)
0 (GPI-Linked Proteins)
0 (Lsb1 protein, S cerevisiae)
0 (MOT3 protein, S cerevisiae)
0 (Molecular Chaperones)
0 (PRND protein, human)
0 (Prions)
0 (RNA-Binding Proteins)
0 (Saccharomyces cerevisiae Proteins)
0 (Transcription Factors)
0 (Whi3 protein, S cerevisiae)
Entry Date(s):
Date Created: 20200908 Date Completed: 20210310 Latest Revision: 20210310
Update Code:
20240105
DOI:
10.1016/j.yexcr.2020.112262
PMID:
32896568
Czasopismo naukowe
Epigenetic modifications allow cells to quickly alter their gene expression and adapt to different stresses. In addition to direct chromatin modifications, prion-like proteins have recently emerged as a system that can sense and adapt the cellular response to stressful conditions. Interestingly, such responses are maintained through prions' self-templating conformations and transmitted to the progeny of the cell that established a prion trait. Alternatively, mnemons are prion-like proteins which conformational switch encodes memories of past events and yet does not propagate to daughter cells. In this review, we explore the biology of the recently described prions found in Saccharomyces cerevisiae including [ESI + ], [SMAUG + ], [GAR + ], [MOT3 + ], [MOD + ], [LSB + ] as well as the Whi3 mnemon. The reversibility of the phenotypes they encode allows cells to remove traits which are no longer adaptive under stress relief and chaperones play a fundamental role in all steps of prion-like proteins functions. Thus, the interplay between chaperones and prion-like proteins provides a framework to establish responses to challenging environments.
(Crown Copyright © 2020. Published by Elsevier Inc. All rights reserved.)

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