ArticleNature communications2024
Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Deciphering the genetic background of an industrial 2-ketogluconic acid-producing strain Pseudomonas plecoglossicida JUIM01 using whole-genome sequencing.Biotechnology for biofuels and bioproducts · 2026Article
- Reprogramming of bacterial virulence by lysine acetylation.Nature communications · 2026Article
- Dynamic acetylation of a conserved lysine impacts glycerol kinase activity and abundance in the haloarchaeon Haloferax volcanii.The Journal of biological chemistry · 2026Article
- Metabolic response ofFrontiers in microbiology · 2026Article
- Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Distribution and diversity of classical deacylases in bacteria.Nature communications · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli TetR-related transcriptional regulator RutR is involved in the coordination of pyrimidine and purine metabolism. Here we report that lysine acetylation modulates RutR function. Applying the genetic code expansion concept, we produced site-specifically lysine-acetylated RutR proteins. The crystal structure of lysine-acetylated RutR reveals how acetylation switches off RutR-DNA-binding. We apply the genetic code expansion concept in E. coli in vivo revealing the consequences of RutR acetylation on the transcriptional level. We propose a model in which RutR acetylation follows different kinetic profiles either reacting non-enzymatically with acetyl-phosphate or enzymatically catalysed by the lysine acetyltransferases PatZ/YfiQ and YiaC. The NAD
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