ArticleCell2012
An α helix to β barrel domain switch transforms the transcription factor RfaH into a translation factor.
Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
159 citing papers in PubMed, 261 citations in OpenAlex.
- RfaH licenses RNA polymerase for long-range transcription.bioRxiv : the preprint server for biology · 2026Article
- AlphaFold reveals but sometimes distorts an organizational principle of protein folding.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of long-range transcription-translation coupling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Selective targeting of a histone-like silencer Sfx to the R6K conjugal transfer operon.Nucleic acids research · 2026Article
- Exploration of the structural and functional diversity in the metamorphic RfaH subfamily.bioRxiv : the preprint server for biology · 2026Article
- Selective targeting of a histone-like silencer Sfx to the R6K conjugal transfer operon.bioRxiv : the preprint server for biology · 2026Article
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- Computational Identification of Potential Shape-Shifting Proteins from Structures.Methods in molecular biology (Clifton, N.J.) · 2026Article
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- Morpheus: a fragment-based algorithm to predict fold-switching behaviour in proteins across proteomes.Bioinformatics (Oxford, England) · 2025Article
- Environmental regulation of toxin production in Bacillus anthracis.PLoS pathogens · 2025Article
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- Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025Article
- A complex between IF2 and NusA suggests early coupling of transcription-translation.Nature communications · 2025Article
- Computational and experimental assessment of key interdomain residues controlling the fold-switch of RfaH.Protein science : a publication of the Protein Society · 2025Article
- Unraveling structural transitions and kinetics along the fold-switching pathway of the RfaH C-terminal domain using exchange-based NMR.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- AlphaFold2's training set powers its predictions of some fold-switched conformations.Protein science : a publication of the Protein Society · 2025Article
- Unveiling the cold reality of metamorphic proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Evolving concepts of the protein universe.iScience · 2025Review
99 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
NusG homologs regulate transcription and coupled processes in all living organisms. The Escherichia coli (E. coli) two-domain paralogs NusG and RfaH have conformationally identical N-terminal domains (NTDs) but dramatically different carboxy-terminal domains (CTDs), a β barrel in NusG and an α hairpin in RfaH. Both NTDs interact with elongating RNA polymerase (RNAP) to reduce pausing. In NusG, NTD and CTD are completely independent, and NusG-CTD interacts with termination factor Rho or ribosomal protein S10. In contrast, RfaH-CTD makes extensive contacts with RfaH-NTD to mask an RNAP-binding site therein. Upon RfaH interaction with its DNA target, the operon polarity suppressor (ops) DNA, RfaH-CTD is released, allowing RfaH-NTD to bind to RNAP. Here, we show that the released RfaH-CTD completely refolds from an all-α to an all-β conformation identical to that of NusG-CTD. As a consequence, RfaH-CTD binding to S10 is enabled and translation of RfaH-controlled operons is strongly potentiated. PAPERFLICK:
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.