Our treasurer, Valerie Carabetta, has been busy. She was promoted this year to associate professor with tenure! Her lab recently published a paper describing the role of Nε -lysine acetylation on the histone-like protein HBsu in Bacillus subtilis in response to antibiotic exposure. They find that specific acetylation patterns on HBsu are crucial for bacterial survival strategies, such as nucleoid compaction and persister cell formation.
- Acetylation of HBsu at specific lysine residues (e.g., K3, K41, K75) is crucial for proper bacterial response to antibiotics, affecting nucleoid compaction and persister cell formation.
- Interfering with HBsu acetylation accelerates bacterial killing rates and increases persister cell formation.
Their work supports the existence of a histone-like code in bacteria, with acetylation playing a regulatory role in antibiotic survival and persistence.
Model of HBsu response to antibiotic stress. (A) A B. subtilis HBsu structural model was generated in PyMOL using the B. stearothermophilus ortholog as a template (PDB 1HUU). The HBsu homodimer is displayed, with one monomer colored in cyan with the acetylated lysine sites (K3, K18, K37, K41, K75, K80, and K86) labeled in pink, and the other monomer colored purple with the acetylated sites labeled yellow. The left panel is a ribbon diagram, and the right shows a space-filling model. (B) During normal, exponential phase growth, HBsu is acetylated in specific patterns over the chromosome (left). In response to antibiotic stress, possibly only those that induce the formation of ROS, HBsu is deacetylated by an unknown KDAC, especially important at K3 and K75, which leads to a more compacted nucleoid (middle). This compaction may protect against further damage and/or change the transcriptional program to aid in survival. When the stress is removed, an unknown KAT acetylates HBsu and acetylation at K41 is likely an important early event to trigger the reentry into growth (right).
Carr RA, Tucker T, Newman PM, Jadalla L, Jaludi K, Reid BE, Alpheaus DN, Korrapati A, Pivonka AE, Carabetta VJ. Nε-lysine acetylation of the histone-like protein HBsu influences antibiotic survival and persistence in Bacillus subtilis. Front Microbiol. 2024 May 21;15:1356733. doi: 10.3389/fmicb.2024.1356733. PMID: 38835483; PMCID: PMC11148388. https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2024.1356733/full
댓글