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In Ukrainian Export citations UNIMARC BibTeX RIS The role of post-translational acetylation in the association of ATG8 autophagia protein with microtubules from plant cells
SUMMARY. At the moment, a number of factors are known that can influence the processes of the cell cycle. One of these factors are post-translational modifications (PTMs) of proteins that cause changes in their structure and, as a consequence, functionality and ability to interact with other proteins of the cell, including microtubule proteins. The aim of our work was a comparative analysis of the mechanism of the effect of PTMs on the structure and activity of proteins by the example of the effect of acetylation of Lys40 in α-tubulin TUBA4 from A. thaliana on its interaction with ATG8à. All the studied proteins were reconstructed by homology to the experimentally proven crystal structures. Further comparative analysis of protein-protein interactions was carried out using in silico methods. We have shown that acetylation of α-tubulin at Lys40 leads to stabilization of its structure in comparison with its non-acetylated form. It was also demonstrated using molecular dynamics that the replacement of acetylated α-tubulin in a complex with ATG8 by its non-acetylated form leads to a reduction in the interacting residues and, as a consequence, to a complete breakdown of the contact. Acetylation of α-tubulin at the Lys40 residue leads to the stabilization of both the protein itself and the complex under study with ATG8. Key words: post-translational modifications, tubulin, ATG8, microtubules, in silico, molecular dynamics
Tsitologiya i Genetika 2021, vol. 55, no. 6, pp. 15-25
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