+検索条件
-Structure paper
タイトル | Transcription termination factor ρ polymerizes under stress. |
---|---|
ジャーナル・号・ページ | bioRxiv, Year 2023 |
掲載日 | 2023年8月18日 |
著者 | Bing Wang / Nelly Said / Tarek Hilal / Mark Finazzo / Markus C Wahl / Irina Artsimovitch / |
PubMed 要旨 | Bacterial RNA helicase ρ is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by ρ is essential for ...Bacterial RNA helicase ρ is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by ρ is essential for quality control of the transcriptome during optimal growth. However, it is unclear how bacteria protect their RNAs from overzealous ρ during dormancy or stress, conditions common in natural habitats. Here we used cryogenic electron microscopy, biochemical, and genetic approaches to show that residue substitutions, ADP, or ppGpp promote hyper-oligomerization of ρ. Our results demonstrate that nucleotides bound at subunit interfaces control ρ switching from active hexamers to inactive higher-order oligomers and extended filaments. Polymers formed upon exposure to antibiotics or ppGpp disassemble when stress is relieved, thereby directly linking termination activity to cellular physiology. Inactivation of ρ through hyper-oligomerization is a regulatory strategy shared by RNA polymerases, ribosomes, and metabolic enzymes across all life. |
リンク | bioRxiv / PubMed:37645988 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 2.63 - 3.5 Å |
構造データ | EMDB-18130, PDB-8q3n: EMDB-18131, PDB-8q3o: EMDB-18132, PDB-8q3p: EMDB-18133, PDB-8q3q: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-0O2: |
由来 |
|
キーワード | TRANSCRIPTION (転写 (生物学)) / Rho / termination |