Electron microscopy studies of protein aggregation and disaggregation

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• Helen Saibil ISMB, Birkbeck College London
• Wednesday 02 March 2016, 10:30-11:30
• Department of Chemistry, Cambridge, Unilever lecture theatre.

If you have a question about this talk, please contact Jerome Charmet.

All welcome

Single particle electron microscopy and electron tomography have been used to study models of protein misfolding, aggregation, and disaggregation. Using a yeast aggregation models, we are examining the structure 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 assembly and disassembly. By an in vitro approach, we have also imaged the mammalian Hsp70 chaperone machinery during disassembly of amyloid fibrils.

References

Carroni, 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

O’Driscoll, J, Clare, DK, Saibil, HR (2015) Remodelling of prion aggregates in yeast cells by the Hsp104-Hsp110 disaggregase machinery. J. Cell Biol. 211, 145-158.

Gao, X Carroni, M, Nussbaum-Krammer, C, Mogk, A, Nillegoda, NB, Szlachcic, A, Guilbride, DL, Saibil, HR, Mayer, MP and Bukau, B (2015) Human Hsp70 disaggregase reverses Parkinson’s-linked α-synuclein amyloid fibrils. Molec. Cell 59, 781-793.

Saibil, HR (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nature Rev. Mol. Cell Biol. 14, 630-642.

Saibil HR, Grünewald K, Stuart DI. (2015) A national facility for biological cryo-electron microscopy. Acta Crystallogr D Biol Crystallogr. 71:127-135.

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