Acetylation of translation machinery affected protein translation in E. coli
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APPLIED MICROBIAL AND CELL PHYSIOLOGY
Acetylation of translation machinery affected protein translation in E. coli Bai-Qing Zhang 1 & Hai-Lei Bu 1 & Di You 1 & Bang-Ce Ye 1,2,3 Received: 5 September 2020 / Revised: 17 October 2020 / Accepted: 26 October 2020 # Springer-Verlag GmbH Germany, part of Springer Nature 2020
Abstract Reversible lysine acetylation (RLA) of translation machinery components, such as ribosomal proteins (RPs) and translation factors (TFs), was identified in many microorganisms, while knowledge of its function and effect on translation remains limited. Herein, we show that translation machinery is regulated by acetylation. Using the cell-free translation system of E. coli, we found that AcP-driven acetylation significantly reduced the relative translation rate, and deacetylation partially restored the translation activity. Hyperacetylation caused by intracellular AcP accumulation or carbon/nitrogen fluctuation (carbon overflow or nitrogen limitation) modulated protein translation in vivo. These results uncovered a critical role of acetylation in translation regulation and indicated that carbon/nitrogen imbalance induced acetylation of ribosome in E. coli and dynamically affected translation rate via a global, uniform manner. Key points • Acetylation of translation machinery directly regulated global translation. • K618 of EF-G, K411, and K464 of S1 are the key points influencing translation rate. • Carbon/nitrogen imbalance triggers AcP-dependent acetylation. Keywords Translation regulation . Acetylation . Protein translation . Post-translational modification
Introduction
Di You and Bang-Ce Ye contributed equally to this work. Supplementary Information The online version contains supplementary material available at https://doi.org/10.1007/s00253-02010985-2. * Di You [email protected] * Bang-Ce Ye [email protected] 1
Laboratory of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, China
2
Institute of Engineering Biology and Health, Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014, Zhejiang, China
3
School of Chemistry and Chemical Engineering, Shihezi University, Xinjiang 832000, China
Proteins, as the material basis of life, bear the main function to exercise life activities and occupy more than half of the cellular biomass and consume nearly two-thirds of the energy for synthesis during cell proliferation (Dai et al. 2016; Li et al. 2014). Protein synthesis (translation) is strictly regulated in response to growth phase and nutritional condition for maintaining cellular homeostasis. Translation is carried out by translational machinery composed of ribosomes, translation factors, and aminoacyl-tRNA synthetases, which is thought to be an overall enzymatic reaction. In this context, every component has an effect on protein translation. Limitation of amino acids ca
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