ArticleNucleic acids research2014
Domain movements of the enhancer-dependent sigma factor drive DNA delivery into the RNA polymerase active site: insights from single molecule studies.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs.Communications biology · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Dynamic action of the Sec machinery during initiation, protein translocation and termination.eLife · 2018Article
- HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly.Nature microbiology · 2017Article
- Kinetics of transcription initiation directed by multiple cis-regulatory elements on the glnAp2 promoter.Nucleic acids research · 2016Article
- The bacterial enhancer-dependent RNA polymerase.The Biochemical journal · 2016Review
- Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation.eLife · 2016Article
- Mutations in RNA Polymerase Bridge Helix and Switch Regions Affect Active-Site Networks and Transcript-Assisted Hydrolysis.Journal of molecular biology · 2015Article
- Genome wide interactions of wild-type and activator bypass forms of σ54.Nucleic acids research · 2015Article
- TRANSCRIPTION. Structures of the RNA polymerase-σ54 reveal new and conserved regulatory strategies.Science (New York, N.Y.) · 2015Article
- Evidence that avian reovirus σNS is an RNA chaperone: implications for genome segment assortment.Nucleic acids research · 2015Article
- A perspective on the enhancer dependent bacterial RNA polymerase.Biomolecules · 2015Review
- Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA+ activator.Nucleic acids research · 2014Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Recognition of bacterial promoters is regulated by two distinct classes of sequence-specific sigma factors, σ(70) or σ(54), that differ both in their primary sequence and in the requirement of the latter for activation via enhancer-bound upstream activators. The σ(54) version controls gene expression in response to stress, often mediating pathogenicity. Its activator proteins are members of the AAA+ superfamily and use adenosine triphosphate (ATP) hydrolysis to remodel initially auto-inhibited holoenzyme promoter complexes. We have mapped this remodeling using single-molecule fluorescence spectroscopy. Initial remodeling is nucleotide-independent and driven by binding both ssDNA during promoter melting and activator. However, DNA loading into the RNA polymerase active site depends on co-operative ATP hydrolysis by the activator. Although the coupled promoter recognition and melting steps may be conserved between σ(70) and σ(54), the domain movements of the latter have evolved to require an activator ATPase.
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