ArticleNucleic acids research2013
Interdomain contacts control folding of transcription factor RfaH.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Article
- A contact-based analysis of local energetic frustration dynamics identifies key residues enabling RfaH fold-switch.Protein science : a publication of the Protein Society · 2024Article
- Concerted transformation of a hyper-paused transcription complex and its reinforcing protein.Nature communications · 2024Article
- Local energetic frustration conservation in protein families and superfamilies.Nature communications · 2023Article
- Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Exploring the structural acrobatics of fold-switching proteins using simplified structure-based models.Biophysical reviews · 2023Review
- Article
- Coevolution-derived native and non-native contacts determine the emergence of a novel fold in a universally conserved family of transcription factors.Protein science : a publication of the Protein Society · 2022Article
- Metamorphic proteins under a computational microscope: Lessons from a fold-switching RfaH protein.Computational and structural biotechnology journal · 2022Review
- The N-terminal domain of RfaH plays an active role in protein fold-switching.PLoS computational biology · 2021Article
- Differential Local Stability Governs the Metamorphic Fold Switch of Bacterial Virulence Factor RfaH.Biophysical journal · 2020Article
- NusG, an Ancient Yet Rapidly Evolving Transcription Factor.Frontiers in microbiology · 2020Review
- Ligand accessibility to heme cytochrome bJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Ancient Transcription Factors in the News.mBio · 2019Review
- Reversible fold-switching controls the functional cycle of the antitermination factor RfaH.Nature communications · 2019Article
- Article
- Multifunnel Landscape of the Fold-Switching Protein RfaH-CTD.The journal of physical chemistry. B · 2018Article
- Flipping states: a few key residues decide the winning conformation of the only universally conserved transcription factor.Nucleic acids research · 2017Article
- Interdomain salt-bridges in the Ebola virus protein VP40 and their role in domain association and plasma membrane localization.Protein science : a publication of the Protein Society · 2016Article
- Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape.PLoS computational biology · 2015Article
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Authors and funding
5 authors.
Funding
Abstract
Escherichia coli RfaH activates gene expression by tethering the elongating RNA polymerase to the ribosome. This bridging action requires a complete refolding of the RfaH C-terminal domain (CTD) from an α-helical hairpin, which binds to the N-terminal domain (NTD) in the free protein, to a β-barrel, which interacts with the ribosomal protein S10 following RfaH recruitment to its target operons. The CTD forms a β-barrel when expressed alone or proteolytically separated from the NTD, indicating that the α-helical state is trapped by the NTD, perhaps co-translationally. Alternatively, the interdomain contacts may be sufficient to drive the formation of the α-helical form. Here, we use functional and NMR analyses to show that the denatured RfaH refolds into the native state and that RfaH in which the order of the domains is reversed is fully functional in vitro and in vivo. Our results indicate that all information necessary to determine its fold is encoded within RfaH itself, whereas accessory factors or sequential folding of NTD and CTD during translation are dispensable. These findings suggest that universally conserved RfaH homologs may change folds to accommodate diverse interaction partners and that context-dependent protein refolding may be widespread in nature.
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