ArticleThe Journal of biological chemistry2014
Promoter activation by CII, a potent transcriptional activator from bacteriophage 186.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Phylogenetic Relationships and Evolution of the GenusViruses · 2024Article
- Analysis of Infection Time Courses Shows CII Levels Determine the Frequency of Lysogeny in Phage 186.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186.Nucleic acids research · 2020Article
- RNA polymerase pausing at a protein roadblock can enhance transcriptional interference by promoter occlusion.FEBS letters · 2019Article
- Cis-Antisense Transcription Gives Rise to Tunable Genetic Switch Behavior: A Mathematical Modeling Approach.PloS one · 2015Article
- Bacteriophage P2.BacteriophageReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lysogeny promoting protein CII from bacteriophage 186 is a potent transcriptional activator, capable of mediating at least a 400-fold increase in transcription over basal activity. Despite being functionally similar to its counterpart in phage λ, it shows no homology at the level of protein sequence and does not belong to any known family of transcriptional activators. It also has the unusual property of binding DNA half-sites that are separated by 20 base pairs, center to center. Here we investigate the structural and functional properties of CII using a combination of genetics, in vitro assays, and mutational analysis. We find that 186 CII possesses two functional domains, with an independent activation epitope in each. 186 CII owes its potent activity to activation mechanisms that are dependent on both the σ(70) and α C-terminal domain (αCTD) components of RNA polymerase, contacting different functional domains. We also present evidence that like λ CII, 186 CII is proteolytically degraded in vivo, but unlike λ CII, 186 CII proteolysis results in a specific, transcriptionally inactive, degradation product with altered self-association properties.
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Registered trials
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