Proceedings of the National Academy of SciencesMolecular BiologyPeer-reviewed journal article
Structural basis of long-range transcription-translation coupling
Chengyuan WangiD, Vadim MolodtsoviD, Shashank Shandilya, Linlin YouiD, Jing Zhang, Konstantin KuznedeloviD, Bryce E. NickelsiD, Jason T. KaelberiD, Gregor BlahaiD, Richard H. EbrightiD
Abstract
Structures recently have been reported of molecular assemblies that mediate transcription-translation coupling in Escherichia coli. In these molecular assemblies, termed "coupled transcription-translation complexes" or "TTC-B", RNA polymerase (RNAP) directly interacts with the ribosome, the transcription elongation factor NusG or its paralog RfaH forms a bridge between RNAP and ribosome, and the transcription elongation factor NusA optionally forms a second bridge between RNAP and ribosome. Here, we report structures of coupled transcription-translation complexes having mRNA spacers between RNAP and ribosome longer than the maximum-length mRNA spacer compatible with formation of TTC-B. The results define a new class of coupled transcription-translation complex, termed "TTC-LC," where "LC" denotes "long-range coupling." TTC-LC differs from TTC-B by a [~]60{degrees} rotation and [~]70 [A] translation of RNAP relative to ribosome, resulting in loss of direct interactions between RNAP and ribosome and creation of a [~]70 [A] gap between RNAP and ribosome. TTC-LC accommodates long mRNA spacers by looping out mRNA from the gap between RNAP and ribosome. We present evidence that TTC-LC is an intermediate in assembling and disassembling TTC-B, mediating pre-TTC-B transcription-translation coupling before a ribosome catches up to RNAP, and mediating post-TTC-B transcription-translation coupling after a ribosome stops moving and RNAP continues moving. We show that TTC-B, but not TTC-LC, is severely defective in intrinsic, RNA-hairpin-dependent termination, and that both TTC-B and TTC-LC are severely defective in Rho-dependent termination.
- organism: E. coli
- assay: protein structure
- research focus: protein structure prediction
- approach: statistical model
- approach: experimental assay
- Citations
- 8
- FWCI
- 4.18
- Field percentile
- top 9%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Structural basis of transcription-translation coupling
Chengyuan Wang, Vadim Molodtsov, … Richard H. Ebright·SciencePeer-reviewed·Aug 20, 2020
- Structural basis of translation in transcription-translation coupling
Jing Zhang, Guo‐Liang Lu, … Chengyuan Wang·bioRxiv·Mar 13, 2024
- Structural insight into bacterial co-transcriptional translation initiation
Takeshi Yokoyama, Yuko Murayama, … Shun‐ichi Sekine·bioRxiv·Mar 19, 2024
- Tracking transcription-translation coupling in real-time
N. S. Qureshi, O. Duss·bioRxiv·Dec 7, 2023
- Structural basis of RfaH-mediated transcription-translation coupling
Vadim Molodtsov, Chengyuan Wang, … Richard H. Ebright·Nature Structural & Molecular BiologyPeer-reviewed·Aug 8, 2024
- Escherichia coli NusG links the lead ribosome with the transcription elongation complex
Robert S. Washburn, Philipp Konrad Zuber, … Joachim Frank·iSciencePeer-reviewed·Jul 9, 2020