ArticleJournal of bacteriology2005
A gyrase mutant with low activity disrupts supercoiling at the replication terminus.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Mechanisms of action of ribosomally synthesized and posttranslationally modified peptides (RiPPs).Journal of industrial microbiology & biotechnology · 2021Review
- Supercoil Levels inMicroorganisms · 2019Article
- Species-specific supercoil dynamics of the bacterial nucleoid.Biophysical reviews · 2016Article
- Topological Behavior of Plasmid DNA.Microbiology spectrum · 2015Review
- RNA polymerase: chromosome domain boundary maker and regulator of supercoil density.Current opinion in microbiology · 2014Review
- Single-molecule studies on the mechanical interplay between DNA supercoiling and H-NS DNA architectural properties.Nucleic acids research · 2014Article
- Rates of gyrase supercoiling and transcription elongation control supercoil density in a bacterial chromosome.PLoS genetics · 2012Article
- Article
- Article
- Growth rate toxicity phenotypes and homeostatic supercoil control differentiate Escherichia coli from Salmonella enterica serovar Typhimurium.Journal of bacteriology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
When a mutation in an essential gene shows a temperature-sensitive phenotype, one usually assumes that the protein is inactive at nonpermissive temperature. DNA gyrase is an essential bacterial enzyme composed of two subunits, GyrA and GyrB. The gyrB652 mutation results from a single base change that substitutes a serine residue for arginine 436 (R436-S) in the GyrB protein. At 42 degrees C, strains with the gyrB652 allele stop DNA replication, and at 37 degrees C, such strains grow but have RecA-dependent SOS induction and show constitutive RecBCD-dependent DNA degradation. Surprisingly, the GyrB652 protein is not inactive at 42 degrees C in vivo or in vitro and it doesn't directly produce breaks in chromosomal DNA. Rather, this mutant has a low k(cat) compared to wild-type GyrB subunit. With more than twice the normal mean number of supercoil domains, this gyrase hypomorph is prone to fork collapse and topological chaos near the terminus of DNA replication.
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Registered trials
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