Literature DB >> 29898402

Different Material States of Pub1 Condensates Define Distinct Modes of Stress Adaptation and Recovery.

Sonja Kroschwald1, Matthias C Munder1, Shovamayee Maharana1, Titus M Franzmann1, Doris Richter1, Martine Ruer1, Anthony A Hyman1, Simon Alberti2.   

Abstract

How cells adapt to varying environmental conditions is largely unknown. Here, we show that, in budding yeast, the RNA-binding and stress granule protein Pub1 has an intrinsic property to form condensates upon starvation or heat stress and that condensate formation is associated with cell-cycle arrest. Release from arrest coincides with condensate dissolution, which takes minutes (starvation) or hours (heat shock). In vitro reconstitution reveals that the different dissolution rates of starvation- and heat-induced condensates are due to their different material properties: starvation-induced Pub1 condensates form by liquid-liquid demixing and subsequently convert into reversible gel-like particles; heat-induced condensates are more solid-like and require chaperones for disaggregation. Our data suggest that different physiological stresses, as well as stress durations and intensities, induce condensates with distinct physical properties and thereby define different modes of stress adaptation and rates of recovery.
Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Hsp104; condensate; cytosolic pH; molecular chaperone; phase separation; phase transition; protein aggregation; stress granule; stress response

Mesh:

Substances:

Year:  2018        PMID: 29898402     DOI: 10.1016/j.celrep.2018.05.041

Source DB:  PubMed          Journal:  Cell Rep            Impact factor:   9.423


  63 in total

1.  Tug of War between Condensate Phases in a Minimal Macromolecular System.

Authors:  Archishman Ghosh; Xiaojia Zhang; Huan-Xiang Zhou
Journal:  J Am Chem Soc       Date:  2020-05-04       Impact factor: 15.419

2.  Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.

Authors:  Jeremy J Ryan; Macy L Sprunger; Kayla Holthaus; James Shorter; Meredith E Jackrel
Journal:  J Biol Chem       Date:  2019-06-05       Impact factor: 5.157

Review 3.  Cellular sensing by phase separation: Using the process, not just the products.

Authors:  Haneul Yoo; Catherine Triandafillou; D Allan Drummond
Journal:  J Biol Chem       Date:  2019-03-15       Impact factor: 5.157

Review 4.  Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.

Authors:  James Shorter; Daniel R Southworth
Journal:  Cold Spring Harb Perspect Biol       Date:  2019-08-01       Impact factor: 10.005

Review 5.  The molecular language of membraneless organelles.

Authors:  Edward Gomes; James Shorter
Journal:  J Biol Chem       Date:  2018-07-25       Impact factor: 5.157

Review 6.  Who's In and Who's Out-Compositional Control of Biomolecular Condensates.

Authors:  Jonathon A Ditlev; Lindsay B Case; Michael K Rosen
Journal:  J Mol Biol       Date:  2018-08-09       Impact factor: 5.469

7.  Determinants for Fusion Speed of Biomolecular Droplets.

Authors:  Archishman Ghosh; Huan-Xiang Zhou
Journal:  Angew Chem Int Ed Engl       Date:  2020-09-08       Impact factor: 15.336

8.  Heterochromatin Protein HP1α Gelation Dynamics Revealed by Solid-State NMR Spectroscopy.

Authors:  Bryce E Ackermann; Galia T Debelouchina
Journal:  Angew Chem Int Ed Engl       Date:  2019-04-03       Impact factor: 15.336

9.  Structural and mechanistic insights into Hsp104 function revealed by synchrotron X-ray footprinting.

Authors:  Elizabeth A Sweeny; Amber Tariq; Esin Gurpinar; Michelle S Go; Matthew A Sochor; Zhong-Yuan Kan; Leland Mayne; S Walter Englander; James Shorter
Journal:  J Biol Chem       Date:  2019-12-27       Impact factor: 5.157

Review 10.  Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior.

Authors:  Titus M Franzmann; Simon Alberti
Journal:  J Biol Chem       Date:  2018-06-19       Impact factor: 5.157

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