ArticleMolecular microbiology2005
Polyphosphate kinase regulates error-prone replication by DNA polymerase IV in Escherichia coli.
Article in Molecular microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- Sending out an SOS - the bacterial DNA damage response.Genetics and molecular biology · 2022Article
- Model systems for studying polyphosphate biology: a focus on microorganisms.Current genetics · 2021Review
- Degeneration of industrial bacteria caused by genetic instability.World journal of microbiology & biotechnology · 2020Review
- Interactions between DksA and Stress-Responsive Alternative Sigma Factors Control Inorganic Polyphosphate Accumulation in Escherichia coli.Journal of bacteriology · 2020Article
- Inorganic Polyphosphate Accumulation in Escherichia coli Is Regulated by DksA but Not by (p)ppGpp.Journal of bacteriology · 2019Article
- The EnvZ-OmpR Two-Component Signaling System Is Inactivated in a Mutant Devoid of Osmoregulated Periplasmic Glucans inFrontiers in microbiology · 2018Article
- Polyphosphate and associated enzymes as global regulators of stress response and virulence in Campylobacter jejuni.World journal of gastroenterology · 2016Review
- Interactions and Localization of Escherichia coli Error-Prone DNA Polymerase IV after DNA Damage.Journal of bacteriology · 2015Article
- Article
- Competitive fitness during feast and famine: how SOS DNA polymerases influence physiology and evolution in Escherichia coli.Genetics · 2013Article
- in Silico analysis of Escherichia coli polyphosphate kinase (PPK) as a novel antimicrobial drug target and its high throughput virtual screening against PubChem library.Bioinformation · 2013Article
- Stress-Induced Mutagenesis.EcoSal Plus · 2012Article
- Translesion DNA Synthesis.EcoSal Plus · 2012Article
- Culture history and population heterogeneity as determinants of bacterial adaptation: the adaptomics of a single environmental transition.Microbiology and molecular biology reviews : MMBR · 2012Review
- 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
- The transcription elongation factor NusA is required for stress-induced mutagenesis in Escherichia coli.Current biology : CB · 2010Article
- Importance of polyphosphate kinase 1 for Campylobacter jejuni viable-but-nonculturable cell formation, natural transformation, and antimicrobial resistance.Applied and environmental microbiology · 2009Article
- DinB upregulation is the sole role of the SOS response in stress-induced mutagenesis in Escherichia coli.Genetics · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The ppk gene encodes polyphosphate kinase (Ppk), an enzyme that catalyses the polymerization of inorganic phosphate into long chains of polyphosphate (polyP). An insertion mutation in ppk causes a decrease in adaptive mutation in Escherichia coli strain FC40. Adaptive mutation in FC40 mostly results from error-prone DNA polymerase IV (Pol IV), encoded by dinB; most of the antimutagenic phenotype of the ppk mutant disappears in a dinB mutant strain. In addition, the ppk mutant causes a decrease in growth-dependent mutations produced by overexpressing Pol IV. However, the amount of Pol IV protein is unchanged in the ppk mutant strain, indicating that the activity or fidelity of Pol IV is altered. Adaptive mutation is inhibited both by the absence of Ppk, which results in low amounts of polyP, and by overproduction of Ppk, which results in high amounts of polyP, suggesting that an optimal level of polyP is necessary. Taken together, these results suggest a novel mechanism involving polyP that directly or indirectly regulates DNA polymerase activity or fidelity.
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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.