Fig. 1: Identification of the SPZ-1 interacting proteins. | Nature Communications

Fig. 1: Identification of the SPZ-1 interacting proteins.

From: Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds

Fig. 1: Identification of the SPZ-1 interacting proteins.

a The indicated proteins were HA-epitope tagged at their endogenous loci and co-precipitating proteins were identified by mass spectrometry. Double arrows identify mutual co-precipitators. Details are provided in Supplementary Table 1. b Sequence conservation (grey) and coiled-coil probability (black) of the indicated proteins. The horizontal bar above each graph shows the coiled-coil dimer probability according to the greyscale shown in the legend. c The localization of chromosomally-encoded mGFP fusion proteins is shown for the indicated proteins. Dotted white lines show the hyphal outline. Scale bar = 10 μm. d For the indicated strains, the average growth rate is shown as mean values ± SD (n = 3 independent measurements shown as opaque red dots). e The indicated HA-epitope tagged proteins were fused to a C-terminal peroxisome tail-anchor (TAperoxisome) and combined through sexual crosses with the indicated mGFP-fusion proteins. Under this condition, SPZ-1, JNS-1 and SPA-2 can each recruit the others to the surface of the peroxisome. mCherry-PTS1 provides a marker of the peroxisome matrix. Scale bar = 2 μm. f Aberrant peroxisome accumulation at the SPK shows that ectopically assembled complexes are all competent for transport. The no ectopic panel shows the normal distribution of peroxisomes. Dotted white lines show the hyphal outline. Scale bar = 10 μm. Source data are provided as a Source Data file.

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