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Structural and functional features of lysine acetylation of plant and animal tubulins

Journal Article · · Cell Biology International
DOI:https://doi.org/10.1002/cbin.10887· OSTI ID:1409472
 [1];  [2];  [1];  [1];  [1]
  1. Laboratory of Structural Biology, Institute of Food Biotechnology and Genomics National Academy of Sciences of Ukraine Kyiv 04123 Ukraine
  2. Medway School of Pharmacy Universities of Kent and Greenwich Kent ME4 4TB UK
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Abstract

The study of the genome and the proteome of different species and representatives of distinct kingdoms, especially detection of proteome via wide‐scaled analyses has various challenges and pitfalls. Attempts to combine all available information together and isolate some common features for determination of the pathway and their mechanism of action generally have a highly complicated nature. However, microtubule (MT) monomers are highly conserved protein structures, and microtubules are structurally conserved from Homo sapiens to Arabidopsis thaliana . The interaction of MT elements with microtubule‐associated proteins and post‐translational modifiers is fully dependent on protein interfaces, and almost all MT modifications are well described except acetylation. Crystallography and interactome data using different approaches were combined to identify conserved proteins important in acetylation of microtubules. Application of computational methods and comparative analysis of binding modes generated a robust predictive model of acetylation of the ϵ‐amino group of Lys40 in α‐tubulins. In turn, the model discarded some probable mechanisms of interaction between elements of interest. Reconstruction of unresolved protein structures was carried out with modeling by homology to the existing crystal structure (PDBID: 1Z2B) from B. taurus using Swiss‐model server, followed by a molecular dynamics simulation. Docking of the human tubulin fragment with Lys40 into the active site of α‐tubulin acetyltransferase, reproduces the binding mode of peptidomimetic from X‐ray structure (PDBID: 4PK3).

Sponsoring Organization:
USDOE
OSTI ID:
1409472
Journal Information:
Cell Biology International, Journal Name: Cell Biology International Journal Issue: 9 Vol. 43; ISSN 1065-6995
Publisher:
Wiley Blackwell (John Wiley & Sons)Copyright Statement
Country of Publication:
Country unknown/Code not available
Language:
English

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