Research groups

Research

Molecular chaperones and protein quality control.

The work of my group focuses on studies of molecular chaperone action in cellular protein folding and misfolding. Protein folding is not always an efficient process and may result in the formation of insoluble aggregates. In vivo this becomes a major problem under conditions of cellular stress, such as heat, cold, chemicals etc. There are also a number of amyloid diseases which occur due to the formation of fibrillar structures composed of ordered protein aggregates. Molecular chaperones, many of which are heat-shock proteins, are required to ensure that proteins are correctly refolded to their native states or targetted for degradation after they have misfolded or aggregated. Thus they play a vital role in the protein quality control within the cell.

Structures of E. coli ClpB and E. coli GroEL

Group

Tom Piggott and Skye Hodson.

Recent publications

Krzewska J, Tanaka M, Burston S.G., Melki R. (2007) Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. Journal of Biological Chemistry. 282, 1679-1686.

Cliff, M.J., Limpkin, C., Cameron, A., Burston, S.G. & Clarke, A. R. (2006) Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. Journal of Biological Chemistry. 281, 21266-21275.

Burston, S.G., Clarke, A.R. & Bigotti, M.G. (2006) The Hsp60 chaperonins from prokaryotes and eukaryotes. in “Chaperones” eds. M. Makarow & I. Braakman. Topics in Current Genetics. pp 253-287. ISBN: 3-540-32580-8.

Poso D, Clarke AR, Burston SG. (2004) A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL. J Mol Biol.338, 969-977.