Nature communications, 2019-02, Vol.10 (1), p.702-702, Article 702
2019
Details
- Autor(en) / Beteiligte
- Titel
- Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
- Ist Teil von
- Nature communications, 2019-02, Vol.10 (1), p.702-702, Article 702
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2019
- Link zum Volltext
- Quelle
- Alma/SFX Local Collection
- Beschreibungen/Notizen
- RfaH, member of the NusG/Spt5 family, activates virulence genes in Gram-negative pathogens. RfaH exists in two states, with its C-terminal domain (CTD) folded either as α-helical hairpin or β-barrel. In free RfaH, the α-helical CTD interacts with, and masks the RNA polymerase binding site on, the N-terminal domain, autoinhibiting RfaH and restricting its recruitment to opsDNA sequences. Upon activation, the domains separate and the CTD refolds into the β-barrel, which recruits a ribosome, activating translation. Using NMR spectroscopy, we show that only a complete ops-paused transcription elongation complex activates RfaH, probably via a transient encounter complex, allowing the refolded CTD to bind ribosomal protein S10. We also demonstrate that upon release from the elongation complex, the CTD transforms back into the autoinhibitory α-state, resetting the cycle. Transformation-coupled autoinhibition allows RfaH to achieve high specificity and potent activation of gene expression.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/s41467-019-08567-6Titel-ID: cdi_doaj_primary_oai_doaj_org_article_daefa0dcbec247efbb406bb9ab9188b3
- Format
- –
- Schlagworte
- Activation, Bacterial Proteins - genetics, Bacterial Proteins - metabolism, Binding sites, DNA-Binding Proteins - metabolism, DNA-directed RNA polymerase, DNA-Directed RNA Polymerases - metabolism, Domains, Elongation, Escherichia coli - genetics, Escherichia coli - metabolism, Escherichia coli Proteins - genetics, Escherichia coli Proteins - metabolism, Gene expression, Gene Expression Regulation, Bacterial, Genetic transformation, Magnetic resonance spectroscopy, Masks, Molecular Dynamics Simulation, NMR spectroscopy, Peptide Elongation Factors - genetics, Peptide Elongation Factors - metabolism, Protein Binding, Protein Biosynthesis, Protein Folding, Protein Interaction Domains and Motifs, Protein Structure, Tertiary, Proteins, Ribonucleic acid, Ribosomal protein S10, Ribosomal Proteins, Ribosomes, RNA, RNA polymerase, RNA-Binding Proteins - genetics, RNA-Binding Proteins - metabolism, Trans-Activators - genetics, Trans-Activators - metabolism, Transcription elongation, Transcription Factors - metabolism, Transcription, Genetic, Virulence, Virulence - genetics