Journal
NATURE CHEMICAL BIOLOGY
Volume 18, Issue 2, Pages 142-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41589-021-00906-3
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Funding
- National Natural Science Foundation of China [21874100, 22074103, 32101023, 21904097, 22004091]
- Talent Excellence Program from Tianjin Medical University
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Protein lysine 2-hydroxyisobutyrylation (Khib) plays a critical role in the regulation of cellular processes, and the RNA acetyltransferase TmcA acts as a Khib transferase in transcription regulation in prokaryotes. TmcA catalyzes Khib to modulate bacterial acid resistance gene transcription and enhance E. coli survival under acid stress.
Protein lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to play a critical role in the regulation of cellular processes. However, the mechanism and functional consequence of Khib in prokaryotes remain unclear. Here we report that TmcA, an RNA acetyltransferase, functions as a lysine 2-hydroxyisobutyryltransferase in the regulation of transcription. We show that TmcA can effectively catalyze Khib both in vitro and intracellularly, and that R502 is a key site for the Khib catalytic activity of TmcA. Using quantitative proteomics, we identified 467 endogenous candidates targeted by TmcA for Khib in Escherichia coli. Interestingly, we demonstrate that TmcA can specifically modulate the DNA-binding activity of H-NS, a nucleoid-associated protein, by catalysis of Khib at K121. Furthermore, this TmcA-targeted Khib regulates transcription of acid-resistance genes and enhances E. coli survival under acid stress. Our study reveals transcription regulation mediated by TmcA-catalyzed Khib for bacterial acid resistance.
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