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. Author manuscript; available in PMC: 2012 Jul 2.
Published in final edited form as: Biochemistry. 2011 Nov 8;50(47):10300–10310. doi: 10.1021/bi2009147

Figure 1.

Figure 1

Hsp70 forms a complex with tau and inhibits aggregation in vitro. (A) His-tagged hTau40 was incubated with untagged Hsp70 (HSPA1A). Reaction mixtures were incubated with TALON metal affinity resin, which interacts with the His tag located on tau. Proteins bound to the resin were immunoblotted for Hsp70 and tau. The Hsp70 alone control confirms that Hsp70 does not bind nonspecifically to the resin. In the presence of tau, Hsp70 is detected in the elution fraction. (B) Intensity of right angle light scattering as a function of time. Each time point is the average of at least three independent experiments and is represented as the mean ± SEM: (■) Tau alone (2 μM), (◯) 1:128 Hsp70:tau ratio, (▲) 1:64 Hsp70:tau ratio, (◇) 1:32 Hsp70:tau ratio, (▼) 1:16 Hsp70:tau ratio, (□) 1:8 Hsp70:tau ratio, and (●) 1:4 Hsp70:tau ratio. (C) Representative electron micrographs of aggregation reactions at equilibrium (t = 300 min). Note the decreased level of formation of filamentous aggregates while some oligomeric aggregates persist even at the highest concentrations tested. The scale bar is 500 nm. The bottom right image (–Tau) is Hsp70 in aggregation buffer (+AA) in the absence of tau.