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Lysine acetylation of the housekeeping sigma factor enhances the activity of the RNA polymerase holoenzyme

Authors
 Ji-Eun Kim  ;  Joon-Sun Choi  ;  Jong-Seo Kim  ;  You-Hee Cho  ;  Jung-Hye Roe 
Citation
 NUCLEIC ACIDS RESEARCH, Vol.48(5) : 2401-2411, 2020-03 
Journal Title
NUCLEIC ACIDS RESEARCH
ISSN
 0305-1048 
Issue Date
2020-03
MeSH
Acetylation ; Amino Acid Sequence ; Bacterial Proteins / metabolism ; DNA-Directed RNA Polymerases / metabolism* ; Gene Expression Regulation, Bacterial ; Genes, Essential* ; Holoenzymes / metabolism* ; Lysine / metabolism* ; Mutation / genetics ; Promoter Regions, Genetic ; Protein Binding ; Sigma Factor / chemistry ; Sigma Factor / metabolism* ; Streptomyces / genetics ; Streptomyces / growth & development ; Streptomyces / metabolism*
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.
Files in This Item:
T9992020415.pdf Download
DOI
10.1093/nar/gkaa011
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/190190
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