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
Persistent Activation of mRNA Translation by Transient Hsp90 Inhibition
Peter Tsvetkov,Timothy J. Eisen,Sven U. Heinrich,Zarina Brune,Erinc Hallacli,Greg A. Newby,Can Kayatekin,David Pincus,Susan Lindquist +8 more
TL;DR: This article showed that transient loss of heat shock protein 90 function can promote a nongenetic inheritance of a translational state affecting specific mRNAs, introducing a mechanism by which Hsp90 can promote phenotypic variation.
4
Huntington’s Disease Studies at the Interface of Chemistry, Physics, and Biology
Kenneth W. Drombosky
- 20 May 2016
TL;DR: In this article, the authors describe mutated htt-exon1 analogs containing only 22-24 glutamine residues that deliver atypical aggregation: a "hyper-amyloid" analog that aggregates into amyloid fibrils comparable to pathogenic huntingtin, and "hypo-AMyloid analogs whose aggregation stops at the non-β oligomer stage".
4
Defining the role of the polyasparagine repeat domain of the S. cerevisiae transcription factor Azf1p.
TL;DR: In this paper, the polyasparagine (polyN) domain plays a subtle role in transcription but is dispensable for Azf1p localization and prion formation, and the polyN domain may be a useful target for engineering yeast strains for fermentation applications and small molecule production.
Expression of Huntingtin and TDP-43 Derivatives in Fission Yeast Can Cause Both Beneficial and Toxic Effects
Luis Marte,Susanna Boronat,Rubén Barrios,Anna Barcons-Simon,Benedetta Bolognesi,Margarita Cabrera,José Ayté,Elena Hidalgo +7 more
TL;DR: This study demonstrates that in general these prion-like proteins do not cause toxicity under normal conditions, and in fact they can protect cells through indirect mechanisms which up-regulate cellular defense pathways.
Prions and chaperones: Outside the fold
TL;DR: The sting of rejection from the Chicago intellectual-property office may have dulled, but Lindquist recognizes and is dismayed by what she sees as a growing incivility among colleagues, a meanness that she thinks threatens the progress of science.
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