A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
Simon Alberti,Randal Halfmann,Oliver D. King,Oliver D. King,Atul Kapila,Susan Lindquist,Susan Lindquist +6 more
TL;DR: A bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions.
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About: This article is published in Cell. The article was published on 03 Apr 2009. and is currently open access. The article focuses on the topics: Fungal prion.
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Citations
A global analysis of low-complexity regions in the Trypanosoma brucei proteome reveals enrichment in the C-terminus of nucleic acid binding proteins providing potential targets of phosphorylation.
Mathieu Cayla,Keith R. Matthews,Alasdair Ivens +2 more
- 18 Nov 2020
TL;DR: The post-translational modifications of LCRs, and in particular the phosphorylation events, could contribute to post- transcriptional gene expression control and the dynamics of protein targeting to membraneless organelles in kinetoplastid parasites.
Chapter 5 – Prions and Prion-Like Phenomena in Epigenetic Inheritance
Tinh-Suong Nguyen,Hervé Lalucque,Fabienne Malagnac,Philippe Silar +3 more
- 01 Jan 2017
TL;DR: It is shown that some non-mendelian inheritance in the yeast Saccharomyces cerevisiae is due to proteins able to switch their structure in an autocatalytic manner, now called prion.
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Identification of New FG-Repeat Nucleoporins with Amyloid Properties
L. G. Danilov,Xenia V Sukhanova,Ekaterina Antonova,Nina P. Trubitsina,Galina A. Zhouravleva,Stanislav A. Bondarev +5 more
TL;DR: In this article , a wide-scale bioinformatic analysis of nucleoporins with FG-repeats (phenylalanine-glycine repeats) was performed.
The Gln3 Transcriptional Regulator of Saccharomyces cerevisiae Manifests Prion-Like Properties upon Overproduction.
TL;DR: The term “conditional prions” is suggested for proteins, whose prion state is maintained exclusively under non-physiological conditions, including infectivity and dependence on the anti-prion agents.
5
Quinary structure kinetically controls protein function and dysfunction
Tarique Khan,Tejbir S. Kandola,Jianzheng Wu,Ellen Ketter,Shriram Venkatesan,Jeffrey J. Lange,Alejandro Rodriguez Gama,Andrew C. Box,Jay R. Unruh,Malcolm Cook,Randal Halfmann +10 more
TL;DR: The results suggest that quinary structure broadly distinguishes the kinetics of subcellular organization, signal propagation, cytoplasmic inheritance, and proteotoxic activities of low complexity “prion-like” sequences.
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