Heat shock proteins (HSPs) are central to the cellular stress response: almost all organisms express an HSP or HSP analog.  HSPs are thought to protect the cell against stress-initiated protein denaturation and aggregation by binding hydrophobic residues exposed upon protein unfolding.   We seek to study the dynamics of this interaction between HSPs and cellular proteins.  We use FRET paired fluorescent proteins to label a destabilized mutant of phosphoglycerate kinase (PGK) and Hsp-70.  PGK unfolding is initiated by a temperature jump and binding is monitored via the change in FRET efficiency.  We find that Hsp-70 binds PGK at its melting point both in vitro and in vivo and we observe heterogeneous, temperature dependent binding kinetics.  These results and future experiments will be able to shed light on the molecular mechanism used by HSPs to protect the cell against protein denaturation and aggregation.

Early events in the cell's heat shock response

244th National Meeting (2012)

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