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SUMMARY:Electron microscopy studies of protein aggregation and disaggregat
 ion - Helen Saibil ISMB\, Birkbeck College London
DTSTART:20160302T103000Z
DTEND:20160302T113000Z
UID:TALK64892@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:Single particle electron microscopy and electron tomography ha
 ve been used to study models of protein misfolding\, aggregation\, and dis
 aggregation. Using a yeast aggregation models\, we are examining the struc
 ture of amyloid and other deposits in situ. For a yeast [PSI+] prion model
 \, we examined how the deposits depend on the Hsp70 chaperone system. The 
 expression of individual components of the Hsp70 system was manipulated to
  probe their actions in determining the balance between amyloid fibril ass
 embly and disassembly. By an in vitro approach\, we have also imaged the m
 ammalian Hsp70 chaperone machinery during disassembly of amyloid fibrils. 
 \n\nReferences\n\nCarroni\, M\, Kummer\, E\, Oguchi\, Y\, Wendler\, P\
 , Clare\, DK\, Sinning\, I\, Kopp\, J\, Mogk\, A\, Bukau\, B\, Saibil
 \, H (2014) Head-to-tail interactions of the coiled-coil domains regulate 
 ClpB cooperation with Hsp70 in protein disaggregation. eLife 3:e02481\n\nO
 ’Driscoll\, J\, Clare\, DK\, Saibil\, HR (2015) Remodelling of prion agg
 regates in yeast cells by the Hsp104-Hsp110 disaggregase machinery. J. Cel
 l Biol. 211\, 145-158.\n\nGao\, X Carroni\, M\, Nussbaum-Krammer\, C\, Mog
 k\, A\, Nillegoda\, NB\, Szlachcic\, A\, Guilbride\, DL\, Saibil\, HR\, Ma
 yer\, MP and Bukau\, B (2015) Human Hsp70 disaggregase reverses Parkinson
 ’s-linked α-synuclein amyloid fibrils. Molec. Cell 59\, 781-793.\n\nSai
 bil\, HR (2013) Chaperone machines for protein folding\, unfolding and dis
 aggregation. Nature Rev. Mol. Cell Biol. 14\, 630-642.\n\nSaibil HR\, Grü
 newald K\, Stuart DI. (2015) A national facility for biological cryo-elect
 ron microscopy. Acta Crystallogr D Biol Crystallogr. 71:127-135.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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