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. Author manuscript; available in PMC: 2019 Jun 2.
Published in final edited form as: Biochem Biophys Res Commun. 2018 Apr 17;500(2):423–428. doi: 10.1016/j.bbrc.2018.04.093

Figure 4.

Figure 4

Tarp generates flexible actin bundles. (A) The average length of the actin structures were measured from the TIRF microscopy images where 500 nM of rhodamine labelled F-actin was incubated with or without 500 nM of Tarp or the mutant Tarp proteins. (B) Persistence lengths (Lp) of actin filaments alone, and Tarp-, FAB domain-, α-actinin- or fascin-mediated actin bundles were analyzed ([actin] = 500 nM, [Tarp, FAB or fascin] = 500 nM, for α-actinin, [actin] = 5 μM and [α-actinin] = 1 μM). The data represent the average of three experiments. (C) Persistence length was measured for the actin bundles generated by co-incubation of F-actin and Tarp in three different molar ratios (2:1, 1:1 and 1:3) ([actin] = 500nM). Mann-Whitney test was performed between 2 non-parametric groups. The data plotted as mean ± SD. * = p<0.05.