ArticleThe EMBO journal2005
Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 74 citations in OpenAlex.
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- 1,3-propanediol production by Klebsiella pneumoniae ∆dhaM∆ptsG∆glpK using glucose and glycerol as co-substrates.Microbial cell factories · 2025Article
- Engineering of increased L-Threonine production in bacteria by combinatorial cloning and machine learning.Metabolic engineering communications · 2023Article
- Subtle sequence differences between two interacting σThe FEBS journal · 2022Article
- The reliance of glycerol utilization by Cupriavidus necator on COApplied microbiology and biotechnology · 2022Article
- Gene-gene relationships in anMicrobial genomics · 2021Article
- Comparative Whole Genome Analysis ofFrontiers in microbiology · 2021Article
- Opening a Novel Biosynthetic Pathway to Dihydroxyacetone and Glycerol inInternational journal of molecular sciences · 2020Article
- Bacterial bug-out bags: outer membrane vesicles and their proteins and functions.Journal of microbiology (Seoul, Korea) · 2020Review
- Systematic identification of metabolites controlling gene expression in E. coli.Nature communications · 2019Article
- Chemical and Metabolic Controls on Dihydroxyacetone Metabolism Lead to Suboptimal Growth of Escherichia coli.Applied and environmental microbiology · 2019Article
- High-yield production of 1,3-propanediol from glycerol by metabolically engineeredBiotechnology for biofuels · 2018Article
- Identification of new Corynebacterium pseudotuberculosis antigens by immunoscreening of gene expression library.BMC microbiology · 2017Article
- Regulation ofEcoSal Plus · 2017Review
- Metabolic engineering of a glycerol-oxidative pathway in Lactobacillus panis PM1 for utilization of bioethanol thin stillage: potential to produce platform chemicals from glycerol.Applied and environmental microbiology · 2014Article
- Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureus.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A genome-scale metabolic flux model of Escherichia coli K-12 derived from the EcoCyc database.BMC systems biology · 2014Article
- Genomic analysis of the regulatory elements and links with intrinsic DNA structural properties in the shrunken genome of Buchnera.BMC genomics · 2013Article
- Genetic engineering of the phosphocarrier protein NPr of the Escherichia coli phosphotransferase system selectively improves sugar uptake activity.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dihydroxyacetone (Dha) kinases are a sequence-conserved family of enzymes, which utilize either ATP (in animals, plants, bacteria) or the bacterial phosphoenolpyruvate carbohydrate phosphotransferase system (PTS) as a source of high-energy phosphate. The PTS-dependent kinase of Escherichia coli consists of three subunits: DhaK contains the Dha binding site, DhaL contains ADP as cofactor for the double displacement of phosphate from DhaM to Dha, and DhaM provides a phospho-histidine relay between the PTS and DhaL::ADP. DhaR is a transcription activator belonging to the AAA+ family of enhancer binding proteins. It stimulates transcription of the dhaKLM operon from a sigma70 promoter and autorepresses dhaR transcription. Genetic and biochemical studies indicate that the enzyme subunits DhaL and DhaK act antagonistically as coactivator and corepressor of the transcription activator by mutually exclusive binding to the sensing domain of DhaR. In the presence of Dha, DhaL is dephosphorylated and DhaL::ADP displaces DhaK and stimulates DhaR activity. In the absence of Dha, DhaL::ADP is converted by the PTS to DhaL::ATP, which does not bind to DhaR.
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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.