Structural basis of the substrate specificity of the alpha-tubulin acetyltransferase

2016 Fiscal Year Final Research Report

• Project/Area Number: 26440033
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Kyushu University
• Principal Investigator: Yuzawa Satoru 九州大学, 医学研究院, 共同研究員 (40515029)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: 翻訳後修飾 / 微小管 / 酵素 / 基質特異性 / X線結晶構造解析

Outline of Final Research Achievements

The functions of microtubules are controlled in part by tubulin post-translational modification. αTAT1 is the major α-tubulin acetyltransferase in ciliated organisms and acetylates conserved lysine residue at lysine 40 on α-tubulin proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine. In this study, we determined the crystal structures of αTAT1 bound to its substrate acetyl-CoA or CoA and show the cofactor-mediated stabilization of αTAT1．We also elucidate the recognition of α-tubulin by αTAT1 using wild type and mutant proteins and study on structure of the CoA disulfide bound αTAT1.

Free Research Field

構造生物学