ArticleMolecular microbiology2010
Functional regions of the N-terminal domain of the antiterminator RfaH.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 73 citations in OpenAlex.
- Exploration of the structural and functional diversity in the metamorphic RfaH subfamily.bioRxiv : the preprint server for biology · 2026Article
- Computational and experimental assessment of key interdomain residues controlling the fold-switch of RfaH.Protein science : a publication of the Protein Society · 2025Article
- Reciprocating RNA Polymerase batters through roadblocks.Nature communications · 2024Article
- Concerted transformation of a hyper-paused transcription complex and its reinforcing protein.Nature communications · 2024Article
- Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis.Molecular cell · 2023Article
- 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
- NusG-dependent RNA polymerase pausing is a frequent function of this universally conserved transcription elongation factor.Critical reviews in biochemistry and molecular biology · 2020Article
- Article
- High intrinsic hydrolytic activity of cyanobacterial RNA polymerase compensates for the absence of transcription proofreading factors.Nucleic acids research · 2020Article
- Differential Local Stability Governs the Metamorphic Fold Switch of Bacterial Virulence Factor RfaH.Biophysical journal · 2020Article
- Ancient Transcription Factors in the News.mBio · 2019Review
- In silico discovery of small molecules that inhibit RfaH recruitment to RNA polymerase.Molecular microbiology · 2018Article
- Locking the nontemplate DNA to control transcription.Molecular microbiology · 2018Article
- Reading of the non-template DNA by transcription elongation factors.Molecular microbiology · 2018Article
- Article
- Article
- Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.Nucleic acids research · 2017Article
- Flipping states: a few key residues decide the winning conformation of the only universally conserved transcription factor.Nucleic acids research · 2017Article
- Genome Sequence of Pseudomonas stutzeri 273 and Identification of the Exopolysaccharide EPS273 Biosynthesis Locus.Marine drugs · 2017Article
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4 authors at 1 institution in 1 country.
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Abstract
RfaH is a bacterial elongation factor that increases expression of distal genes in several long, horizontally acquired operons. RfaH is recruited to the transcription complex during RNA chain elongation through specific interactions with a DNA element called ops. Following recruitment, RfaH remains bound to RNA polymerase (RNAP) and acts as an antiterminator by reducing RNAP pausing and termination at some factor-independent and Rho-dependent signals. RfaH consists of two domains connected by a flexible linker. The N-terminal RfaH domain (RfaH(N)) recognizes the ops element, binds to the RNAP and reduces pausing and termination in vitro. Functional analysis of single substitutions in this domain reported here suggests that three separate RfaH(N) regions mediate these functions. We propose that a polar patch on one side of RfaH(N) interacts with the non-template DNA strand during recruitment, whereas a hydrophobic surface on the opposite side of RfaH(N) remains bound to the beta' subunit clamp helices domain throughout transcription of the entire operon. The third region is apparently dispensable for RfaH binding to the transcription complex but is required for the antitermination modification of RNAP.
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