Abstract Our study was aimed to anlayze the mechanism of the effect of acetylation of the Lys40 residue in α-tubulin TUBA4 from A. thaliana on its structure and interaction with ATG8a autophagy protein. Reconstruction of the spatial structures of the studied proteins was carried out by homology using experimentally proven crystal structures as a template. Studies of protein–protein interactions and their comparative analysis were performed using in silico methods. It has been demonstrated that acetylation of α-tubulin on the Lys40 residue leads to stabilization of its structure in comparison with its deacetylated form. Also, the analysis of the results of molecular dynamics calculation showed that the replacement of acetylated α-tubulin in complex with ATG8 protein to nonacetylated form leads to a decrease in the number of contact amino acid residues that, as a result, destabilizes the entire complex. Therefore, acetylation of α-tubulin on the Lys40 residue leads to stabilization of the protein itself and its complex with the ATG8 protein.
Keywords: posttranslational modifications tubulin ATG8 microtubules in silico molecular dynamics
