Journal
NUCLEIC ACIDS RESEARCH
Volume 48, Issue 5, Pages 2401-2411Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkaa011
Keywords
-
Categories
Funding
- Intelligent Synthetic Biology Center of Global Frontier Project Grant [2011-0031960]
- National Research Foundation of Korea (NRF) [NRF-2017R1A2B3005239]
- National Research Foundation of Korea (NRF)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available