8q3p

Bacterial transcription termination factor Rho G150D mutant bound to ADP; C-terminal 8xHis-tag

spinqualitylabelsall models 8q3p, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8q3p is a 18 chain structure with sequence from Escherichia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.5Å Ligands: ADP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RHO_ECOLI Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884] Publication Abstract from PubMed Bacterial RNA helicase rho is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by rho is essential for quality control of the transcriptome during optimal growth. However, it is unclear how bacteria protect their RNAs from overzealous rho 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 Escherichia coli rho. Our results demonstrate that nucleotides bound at subunit interfaces control rho 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 rho through hyper-oligomerization is a regulatory strategy shared by RNA polymerases, ribosomes, and metabolic enzymes across all life. Transcription termination factor rho polymerizes under stress.,Wang B, Said N, Hilal T, Finazzo M, Wahl MC, Artsimovitch I bioRxiv [Preprint]. 2023 Aug 18:2023.08.18.553922. doi: , 10.1101/2023.08.18.553922. PMID:37645988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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