Extended Data Fig. 9: MTBH1-2 promotes tubulin polymerization and mutation of residues in the three cationic clusters impairs this activity. | Nature Chemical Biology

Extended Data Fig. 9: MTBH1-2 promotes tubulin polymerization and mutation of residues in the three cationic clusters impairs this activity.

From: Structural basis for α-tubulin-specific and modification state-dependent glutamylation

Extended Data Fig. 9: MTBH1-2 promotes tubulin polymerization and mutation of residues in the three cationic clusters impairs this activity.

a. Quantification of tubulin polymerization over time in the absence or presence of MTBH1-2 and the structure-guided MTBH1-2 mutants. b–f. Representative interference reflection microscopy images from one of two independent experiments of reactions containing 10 μM porcine tubulin without MTBH1-2 (b) or with 2.5 μM MTBH1-2 (c), 2.5 μM MTBH1-2 (K490A/K494A) (d), 25 μM MTBH1-2 (K490A/K494A) (e) and 25 μM MTBH1-2 (K490A/K494A/K498A/K502A) (f). Scale bar, 25 μm.

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