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. Author manuscript; available in PMC: 2019 Aug 7.
Published in final edited form as: Structure. 2018 Jul 5;26(8):1116–1126.e4. doi: 10.1016/j.str.2018.05.015

Figure 8. Impact of the PLPP motif on the assembly of Hsp27* oligomers and client protein binding.

Figure 8.

A, Concentration-dependent dissociation of the Hsp27* oligomer into the functionally-active dimer is disrupted when the PLPP sequence is substituted with a tetra-alanine peptide. 100μl of the proteins, at the indicated concentrations, were eluted at room temperature from the SEC column at pH 7.2. B, Binding to bimane-labeled T4L-L99A is highly attenuated for Hsp27*-PLPP/AAAA mutant, which correlates with reduced propensity to form the dimeric species. T4L-L99A (5μM) was incubated with increasing molar excess of Hsp27* (X-axis) for 2hrs at 37 °C in pH 7.2 buffer, and the fluorescence anisotropy (Y-axis) of the labeled substrate T4L-L99A was measured. (See also Figure S7)