Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	A trailing ribosome speeds up RNA polymerase at the expense of transcript fidelity via force and allostery.
Journal, issue, pages	Cell, Vol. 186, Issue 6, Page 1244-1262.e34, Year 2023
Publish date	Mar 16, 2023
Authors	Liang Meng Wee / Alexander B Tong / Alfredo Jose Florez Ariza / Cristhian Cañari-Chumpitaz / Patricia Grob / Eva Nogales / Carlos J Bustamante /
PubMed Abstract	In prokaryotes, translation can occur on mRNA that is being transcribed in a process called coupling. How the ribosome affects the RNA polymerase (RNAP) during coupling is not well understood. Here, ...In prokaryotes, translation can occur on mRNA that is being transcribed in a process called coupling. How the ribosome affects the RNA polymerase (RNAP) during coupling is not well understood. Here, we reconstituted the E. coli coupling system and demonstrated that the ribosome can prevent pausing and termination of RNAP and double the overall transcription rate at the expense of fidelity. Moreover, we monitored single RNAPs coupled to ribosomes and show that coupling increases the pause-free velocity of the polymerase and that a mechanical assisting force is sufficient to explain the majority of the effects of coupling. Also, by cryo-EM, we observed that RNAPs with a terminal mismatch adopt a backtracked conformation, while a coupled ribosome allosterically induces these polymerases toward a catalytically active anti-swiveled state. Finally, we demonstrate that prolonged RNAP pausing is detrimental to cell viability, which could be prevented by polymerase reactivation through a coupled ribosome.
External links	Cell / PubMed:36931247 / PubMed Central
Methods	EM (single particle)
Resolution	3.8 - 7.3 Å
Structure data	29212 8fix EMDB-29212, PDB-8fix: Cryo-EM structure of E. coli RNA polymerase backtracked elongation complex harboring a terminal mismatch Method: EM (single particle) / Resolution: 3.9 Å 29213 8fiy EMDB-29213, PDB-8fiy: Cryo-EM structure of E. coli RNA polymerase Elongation complex in the Transcription-Translation Complex (RNAP in an anti-swiveled conformation) Method: EM (single particle) / Resolution: 7.3 Å 29214 8fiz EMDB-29214, PDB-8fiz: Cryo-EM structure of E. coli 70S Ribosome containing mRNA and tRNA (in the transcription-translation complex) Method: EM (single particle) / Resolution: 3.8 Å EMDB-40178: Cryo-EM composited map of the E. coli transcription-translation complex (RNAP in an anti-swiveled conformation) Method: EM (single particle) / Resolution: 3.8 Å EMDB-40554: Cryo-EM Consensus map of the E. coli transcription-translation complex (RNAP in an anti-swiveled conformation) Method: EM (single particle) / Resolution: 4.5 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry
Source	escherichia coli k-12 (bacteria) escherichia phage lambda (virus) escherichia coli (E. coli)
Keywords	TRANSCRIPTION / RNA polymerase / ribosome / coupling / TRANSCRIPTION/DNA/RNA / TRANSCRIPTION-DNA-RNA complex / TRANSLATION / 70S Ribosome / transcription-translation coupling