ArticleNucleic acids research2019
Structural basis of σ appropriation.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Liquid-liquid phase separation and a phage-encoded inhibitor cooperatively drive transcriptional transition during phage SPO1 infection.Nucleic acids research · 2026Article
- Article
- Aromatic patch in whiB-like transcription factors facilitates primary sigma factor interaction in mycobacterium tuberculosis.Communications biology · 2026Article
- Transcriptional reprogramming by bacteriophage T4: turning the host transcriptional machinery to the dark side.EcoSal Plus · 2025Review
- Crystal structure of MutYX: a novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-oxoguanine recognition sphere.Nucleic acids research · 2025Article
- A phage transcription factor displaces the host σ factor and stabilizes its own σ factor.Nucleic acids research · 2025Article
- Structural basis of three different transcription activation strategies adopted by a single regulator SoxS.Nucleic acids research · 2022Article
- Structural basis of transcription activation by Rob, a pleiotropic AraC/XylS family regulator.Nucleic acids research · 2022Article
- A Novel Family of Winged-Helix Single-Stranded DNA-Binding Proteins from Archaea.International journal of molecular sciences · 2022Article
- Transcriptional control of mycobacterial DNA damage response by sigma adaptation.Science advances · 2021Article
- Structural basis of transcription activation by the global regulator Spx.Nucleic acids research · 2021Article
- Diverse and unified mechanisms of transcription initiation in bacteria.Nature reviews. Microbiology · 2021Review
- The σ Subunit-Remodeling Factors: An Emerging Paradigms of Transcription Regulation.Frontiers in microbiology · 2020Review
- Article
- Region 4 of the RNA polymerase σ subunit counteracts pausing during initial transcription.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage T4 middle promoters are activated through a process called σ appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite extensive biochemical and genetic analyses, puzzle remains, in part, because of a lack of precise structural information for σ appropriation complex. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact σ appropriation complex, comprising AsiA, MotA, Escherichia coli RNA polymerase (RNAP), σ70 and a T4 middle promoter. As expected, AsiA binds to and remodels σ region 4 to prevent its contact with host promoters. Unexpectedly, AsiA undergoes a large conformational change, takes over the job of σ region 4 and provides an anchor point for the upstream double-stranded DNA. Because σ region 4 is conserved among bacteria, other transcription factors may use the same strategy to alter the landscape of transcription immediately. Together, the structure provides a foundation for understanding σ appropriation and transcription activation.
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