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Article

Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli

1
Biotechnology Research Center, The University of Tokyo, Tokyo 113-8657, Japan
2
Department of Biological Science and Technology, Tokyo University of Science, Tokyo 125-8585, Japan
3
Center for Sustainable Resource Science, RIKEN, Saitama 351-0198, Japan
4
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
5
Department of Chemistry, Yale University, New Haven, CT 06520, USA
6
Research Institute for Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan
*
Author to whom correspondence should be addressed.
Genes 2018, 9(10), 473; https://doi.org/10.3390/genes9100473
Received: 14 August 2018 / Revised: 9 September 2018 / Accepted: 21 September 2018 / Published: 28 September 2018
(This article belongs to the Special Issue Synthetic DNA and RNA Programming)
Protein lysine acetylation is a widely conserved posttranslational modification in all three domains of life. Lysine acetylation frequently occurs in aminoacyl-tRNA synthetases (aaRSs) from many organisms. In this study, we determined the impact of the naturally occurring acetylation at lysine-73 (K73) in Escherichia coli class II alanyl-tRNA synthetase (AlaRS) on its alanylation activity. We prepared an AlaRS K73Ac variant in which Nε-acetyl-l-lysine was incorporated at position 73 using an expanded genetic code system in E. coli. The AlaRS K73Ac variant showed low activity compared to the AlaRS wild type (WT). Nicotinamide treatment or CobB-deletion in an E. coli led to elevated acetylation levels of AlaRS K73Ac and strongly reduced alanylation activities. We assumed that alanylation by AlaRS is affected by K73 acetylation, and the modification is sensitive to CobB deacetylase in vivo. We also showed that E. coli expresses two CobB isoforms (CobB-L and CobB-S) in vivo. CobB-S displayed the deacetylase activity of the AlaRS K73Ac variant in vitro. Our results imply a potential regulatory role for lysine acetylation in controlling the activity of aaRSs and protein synthesis. View Full-Text
Keywords: alanyl-tRNA synthetase; class II aminoacyl-tRNA synthetase; expanded genetic code; lysine acetylation; posttranslational modification alanyl-tRNA synthetase; class II aminoacyl-tRNA synthetase; expanded genetic code; lysine acetylation; posttranslational modification
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MDPI and ACS Style

Umehara, T.; Kosono, S.; Söll, D.; Tamura, K. Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli. Genes 2018, 9, 473. https://doi.org/10.3390/genes9100473

AMA Style

Umehara T, Kosono S, Söll D, Tamura K. Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli. Genes. 2018; 9(10):473. https://doi.org/10.3390/genes9100473

Chicago/Turabian Style

Umehara, Takuya; Kosono, Saori; Söll, Dieter; Tamura, Koji. 2018. "Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli" Genes 9, no. 10: 473. https://doi.org/10.3390/genes9100473

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