Structural studies of tubulin modifying enzymes

Microtubules are essental components of the eukaryotc cytoskeleton. They are subjected to a number of post-translatonal modifcatons, which increase their heterogeneity, leading to functonal specializaton. The combinaton of the post-translatonal modifcatons, together with the diferental overexpression of tubulin isotypes, creates the tubulin code. This thesis focuses on detyrosinaton, one of the post-translatonal modifcatons that occur on the C-terminal tail of α-tubulin. Using a combinaton of structural biology tools, including Small angle X-ray scatering and X-ray crystallography, and biochemical and biophysical assays, I present the structure and the mechanism of the two novel tubulin detyrosinatng enzymes, which remained elusive for four decades, and were discovered by our collaborators.