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Quaternary Dynamics And Plasticity Underlie Small Heat Shock Protein Chaperone Function, Florian Stengel, Andrew J. Baldwin, Alexander J. Painter, Nomalie Jaya, Eman Basha, Lewis E. Kay, Elizabeth Vierling, Carol V. Robinson, Justin L. P. Benesch
Quaternary Dynamics And Plasticity Underlie Small Heat Shock Protein Chaperone Function, Florian Stengel, Andrew J. Baldwin, Alexander J. Painter, Nomalie Jaya, Eman Basha, Lewis E. Kay, Elizabeth Vierling, Carol V. Robinson, Justin L. P. Benesch
Elizabeth Vierling
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein aggregation by binding clients destabilized during cellular stress. Here we probe the architecture and dynamics of complexes formed between an oligomeric sHSP and client by employing unique mass spectrometry strategies. We observe over 300 different stoichiometries of interaction, demonstrating that an ensemble of structures underlies the protection these chaperones confer to unfolding clients. This astonishing heterogeneity not only makes the system quite distinct in behavior to ATP-dependent chaperones, but also renders it intractable by conventional structural biology approaches. We find that thermally regulated quaternary dynamics …