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SUMMARY:Protein phase transition: from biology towards new protein materia
 ls - Paolo Arosio\, Dept of Chemistry and Applied Biosciences\, ETH Zurich
DTSTART:20190522T093000Z
DTEND:20190522T103000Z
UID:TALK122749@talks.cam.ac.uk
CONTACT:Gabriella Heller
DESCRIPTION:Cellular organelles can form via phase separation of proteins 
 and nucleic acids. Yet\, the molecular mechanisms that govern the dynamics
  of these membrane-less compartments remain largely elusive. Here\, we ana
 lyze the microscopic processes underlying the phase separation of the DEAD
 -box protein ATPase Dhh1\, which is strongly associated with the formation
  of processing bodies (P-bodies) in yeast. We show that binding to ATP tri
 ggers the reversible formation of protein-rich droplets\, while RNA promot
 es phase separation and maintains the protein dense phase in the liquid st
 ate. These results reveal molecular mechanisms that cells have plausibly d
 eveloped to accurately control the reversible assembly and the biophysical
  properties of P-bodies. Moreover\, we demonstrate the possibility to mimi
 c these mechanisms and induce similar behaviours in synthetic proteins by 
 conjugating low complexity domains to soluble globular regions. We show th
 at these biologically derived molecular adhesives enable
 the self-assem
 bly of these proteins into supramolecular
 architectures via a
 multis
 tep process. This multistep pathway involves an initial liquid−liquid ph
 ase transition\, which creates protein-rich droplets that mature into prot
 ein aggregates over time. These protein aggregates consist of permeable st
 ructures that maintain activity and release active soluble proteins. We fu
 rther demonstrate that this feature\, together with the dynamic state of t
 he initial dense liquid phase\, allows one to directly assemble different 
 globular domains within the same architecture\, thereby enabling the gener
 ation of both static multifunctional biomaterials and dynamic microscale b
 ioreactors.\n\nReferences\nFaltova L.\, Küffner A. et al\, “Multifuncti
 onal Protein Materials and Microreactors using Low Complexity Domains as M
 olecular Adhesives”\, ACS Nano\, 2018\, 12\, 9991-9999\n
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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