ArticleGenetics2007
The Escherichia coli histone-like protein HU has a role in stationary phase adaptive mutation.
Article in Genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Cinnamic-Hydroxamic-Acid Derivatives Exhibit Antibiotic, Anti-Biofilm, and Supercoiling Relaxation Properties by Targeting Bacterial Nucleoid-Associated Protein HU.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Mutation and Recombination Rates Vary Across Bacterial Chromosome.Microorganisms · 2019Review
- Article
- Roles of Nucleoid-Associated Proteins in Stress-Induced Mutagenic Break Repair in Starving Escherichia coli.Genetics · 2015Article
- Interactions and Localization of Escherichia coli Error-Prone DNA Polymerase IV after DNA Damage.Journal of bacteriology · 2015Article
- Stress-Induced Mutagenesis.EcoSal Plus · 2012Article
- Double-Strand Break Repair and Holliday Junction Processing Are Required for Chromosome Processing in Stationary-Phase Escherichia coli Cells.G3 (Bethesda, Md.) · 2011Article
- Escherichia coli Rep DNA helicase and error-prone DNA polymerase IV interact physically and functionally.Molecular microbiology · 2011Article
- The SMC-like protein complex SbcCD enhances DNA polymerase IV-dependent spontaneous mutation in Escherichia coli.Journal of bacteriology · 2011Article
- RpoS, the stress response sigma factor, plays a dual role in the regulation of Escherichia coli's error-prone DNA polymerase IV.Journal of bacteriology · 2010Article
- HU participates in expression of a specific set of genes required for growth and survival at acidic pH in Escherichia coli.Current microbiology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Stationary phase adaptive mutation in Escherichia coli is thought to be a mechanism by which mutation rates are increased during stressful conditions, increasing the possibility that fitness-enhancing mutations arise. Here we present data showing that the histone-like protein, HU, has a role in the molecular pathway by which adaptive Lac(+) mutants arise in E. coli strain FC40. Adaptive Lac(+) mutations are largely but not entirely due to error-prone DNA polymerase IV (Pol IV). Mutations in either of the HU subunits, HUalpha or HUbeta, decrease adaptive mutation to Lac(+) by both Pol IV-dependent and Pol IV-independent pathways. Additionally, HU mutations inhibit growth-dependent mutations without a reduction in the level of Pol IV. These effects of HU mutations on adaptive mutation and on growth-dependent mutations reveal novel functions for HU in mutagenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.