Acetylation of lysine ϵ-amino groups regulates aminoacyl-tRNA synthetase activity in Escherichia coli.

ABSTRACT: Previous proteomic analyses have shown that aminoacyl-tRNA synthetases in many organisms can be modified by acetylation of Lys. In this present study, leucyl-tRNA synthetase and arginyl-tRNA synthetase from Escherichia coli (EcLeuRS and EcArgRS) were overexpressed and purified and found to be acetylated on Lys residues by MS. Gln scanning mutagenesis revealed that Lys⁶¹⁹, Lys⁶²⁴, and Lys⁸⁰⁹ in EcLeuRS and Lys¹²⁶ and Lys⁴⁰⁸ in EcArgRS might play important roles in enzyme activity. Furthermore, we utilized a novel protein expression system to obtain enzymes harboring acetylated Lys at specific sites and investigated their catalytic activity. Acetylation of these Lys residues could affect their aminoacyl

SUBMITTER: Ye Q 

PROVIDER: S-EPMC5481575 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature