Phylogenetic convergence of phase separation and mitotic function in the disordered protein BuGZ

2022 ◽  
Author(s):  
Alexander F. Chin ◽  
Yixian Zheng ◽  
Vincent J. Hilser
Keyword(s):  
Phase Separation ◽  
Disordered Protein

scholarly journals Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci

PLoS Genetics ◽  
2018 ◽  
Vol 14 (7) ◽  
pp. e1007542 ◽  
Author(s):  
Celja J. Uebel ◽  
Dorian C. Anderson ◽  
Lisa M. Mandarino ◽  
Kevin I. Manage ◽  
Stephan Aynaszyan ◽  
...  
Keyword(s):  
Phase Separation ◽  
Small Rna ◽  
Intrinsically Disordered Protein ◽  
Rna Amplification ◽  
Intrinsically Disordered ◽  
Disordered Protein

scholarly journals A modular platform for engineering function of natural and synthetic biomolecular condensates

2021 ◽  
Author(s):  
Keren Lasker ◽  
Steven Boeynaems ◽  
Vinson Lam ◽  
Emma Stainton ◽  
Maarten Jacquemyn ◽  
...  
Keyword(s):  
Phase Separation ◽  
Material Properties ◽  
Asymmetric Cell Division ◽  
Caulobacter Crescentus ◽  
Intrinsically Disordered Protein ◽  
Emergent Properties ◽  
Physiological Importance ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Modular Platform

AbstractPhase separation is emerging as a universal principle for how cells use dynamic subcompartmentalization to organize biochemical reactions in time and space1,2. Yet, whether the emergent physical properties of these biomolecular condensates are important for their biological function remains unclear. The intrinsically disordered protein PopZ forms membraneless condensates at the poles of the bacterium Caulobacter crescentus and selectively sequesters kinase-signaling cascades to regulate asymmetric cell division3–5. By dissecting the molecular grammar underlying PopZ phase separation, we find that unlike many eukaryotic examples, where unstructured regions drive condensation6,7, a structured domain of PopZ drives condensation, while conserved repulsive features of the disordered region modulate material properties. By generating rationally designed PopZ mutants, we find that the exact material properties of PopZ condensates directly determine cellular fitness, providing direct evidence for the physiological importance of the emergent properties of biomolecular condensates. Our work codifies a clear set of design principles illuminating how sequence variation in a disordered domain alters the function of a widely conserved bacterial condensate. We used these insights to repurpose PopZ as a modular platform for generating synthetic condensates of tunable function in human cells.

scholarly journals Correlating Amino Acid Sequence and Solvation to Disordered Protein Collapse Transitions and Phase Separation

2019 ◽  
Vol 116 (3) ◽  
pp. 194a
Author(s):  
Erik W. Martin ◽  
Alex S. Holehouse ◽  
Ivan Peran ◽  
Anne Bremer ◽  
Rohit V. Pappu ◽  
...  
Keyword(s):  
Phase Separation ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disordered Protein ◽  
Collapse Transitions

scholarly journals Viroplasms: Assembly and Functions of Rotavirus Replication Factories

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1349
Author(s):  
Guido Papa ◽  
Alexander Borodavka ◽  
Ulrich Desselberger
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Reverse Genetics ◽  
Intrinsically Disordered Protein ◽  
Structural Proteins ◽  
Virion Assembly ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Infected Cells ◽  
Liquid Liquid Phase Separation

Viroplasms are cytoplasmic, membraneless structures assembled in rotavirus (RV)-infected cells, which are intricately involved in viral replication. Two virus-encoded, non-structural proteins, NSP2 and NSP5, are the main drivers of viroplasm formation. The structures (as far as is known) and functions of these proteins are described. Recent studies using plasmid-only-based reverse genetics have significantly contributed to elucidation of the crucial roles of these proteins in RV replication. Thus, it has been recognized that viroplasms resemble liquid-like protein–RNA condensates that may be formed via liquid–liquid phase separation (LLPS) of NSP2 and NSP5 at the early stages of infection. Interactions between the RNA chaperone NSP2 and the multivalent, intrinsically disordered protein NSP5 result in their condensation (protein droplet formation), which plays a central role in viroplasm assembly. These droplets may provide a unique molecular environment for the establishment of inter-molecular contacts between the RV (+)ssRNA transcripts, followed by their assortment and equimolar packaging. Future efforts to improve our understanding of RV replication and genome assortment in viroplasms should focus on their complex molecular composition, which changes dynamically throughout the RV replication cycle, to support distinct stages of virion assembly.

scholarly journals Dynamic Structural Changes and Thermodynamics in Protein Phase Separation Processes of an Intrinsically Ordered‐Disordered Protein Model

2021 ◽  
Author(s):  
Steffen Lüdeke ◽  
Philipp Lohner ◽  
Lara G. Stühn ◽  
Martin U. Betschart ◽  
Matthias C. Huber ◽  
...  
Keyword(s):  
Phase Separation ◽  
Structural Changes ◽  
Separation Processes ◽  
Disordered Protein ◽  
Protein Model

scholarly journals Phase Separation of Disordered Protein in the Formation of Membrane-Less Organelles

2014 ◽  
Vol 106 (2) ◽  
pp. 35a ◽  
Author(s):  
Timothy J. Nott ◽  
Patrick Farber ◽  
Evangelia Petsalakis ◽  
Dylan Jervis ◽  
Andrew J. Baldwin ◽  
...  
Keyword(s):  
Phase Separation ◽  
Disordered Protein
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