8Q3O の概要
エントリーDOI | 10.2210/pdb8q3o/pdb |
関連するPDBエントリー | 8Q3N |
EMDBエントリー | 18131 |
分子名称 | Transcription termination factor Rho, guanosine 5'-(tetrahydrogen triphosphate) 3'-(trihydrogen diphosphate), MAGNESIUM ION (3 entities in total) |
機能のキーワード | rho, termination, transcription |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 285177.87 |
構造登録者 | |
主引用文献 | Wang, B.,Said, N.,Hilal, T.,Finazzo, M.,Wahl, M.C.,Artsimovitch, I. Transcription termination factor rho polymerizes under stress. Biorxiv, 2023 Cited by PubMed Abstract: 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. PubMed: 37645988DOI: 10.1101/2023.08.18.553922 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3 Å) |
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