ArticleNucleic acids research2020
Lysine acetylation of the housekeeping sigma factor enhances the activity of the RNA polymerase holoenzyme.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Dynamic microfluidic single-cell screening identifies pheno-tuning compounds to potentiate tuberculosis therapy.Nature communications · 2024Article
- Acetylomics reveals an extensive acetylation diversity withinmicroLife · 2024Article
- Review
- Large-scale genetic analysis and biological traits of two SigB factors inFrontiers in microbiology · 2023Article
- Structural basis of Streptomyces transcription activation by zinc uptake regulator.Nucleic acids research · 2022Article
- RIViT-seq enables systematic identification of regulons of transcriptional machineries.Nature communications · 2022Article
- Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.Journal of bacteriology · 2021Review
- The Phage-EncodedViruses · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein lysine acetylation, one of the most abundant post-translational modifications in eukaryotes, occurs in prokaryotes as well. Despite the evidence of lysine acetylation in bacterial RNA polymerases (RNAPs), its function remains unknown. We found that the housekeeping sigma factor (HrdB) was acetylated throughout the growth of an actinobacterium, Streptomyces venezuelae, and the acetylated HrdB was enriched in the RNAP holoenzyme complex. The lysine (K259) located between 1.2 and 2 regions of the sigma factor, was determined to be the acetylated residue of HrdB in vivo by LC-MS/MS analyses. Specifically, the label-free quantitative analysis revealed that the K259 residues of all the HrdB subunits were acetylated in the RNAP holoenzyme. Using mutations that mimic or block acetylation (K259Q and K259R), we found that K259 acetylation enhances the interaction of HrdB with the RNAP core enzyme as well as the binding activity of the RNAP holoenzyme to target promoters in vivo. Taken together, these findings provide a novel insight into an additional layer of modulation of bacterial RNAP activity.
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