ArticleJournal of bacteriology2009
Constitutive mutations in the Escherichia coli AraC protein.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Genetic "expiry-date" circuits control lifespan of synthetic scavenger bacteria for safe bioremediation.Nucleic acids research · 2025Article
- AraC Functional Suppressors of Mutations in the C-Terminal Domain of the RpoA Subunit of theMicroorganisms · 2024Article
- Review
- Topologies of synthetic gene circuit for optimal fold change activation.Nucleic acids research · 2021Article
- Isolating live cells after high-throughput, long-term, time-lapse microscopy.Nature methods · 2020Article
- Arabinose Alters Both Local and Distal H-D Exchange Rates in the Escherichia coli AraC Transcriptional Regulator.Biochemistry · 2019Article
- Rapid Verification of Terminators Using the pGR-Blue Plasmid and Golden Gate Assembly.Journal of visualized experiments : JoVE · 2016Article
- Multilayered genetic safeguards limit growth of microorganisms to defined environments.Nucleic acids research · 2015Article
- Understanding the basis of a class of paradoxical mutations in AraC through simulations.Proteins · 2013Article
- Mutational analysis of the N-terminal domain of UreR, the positive transcriptional regulator of urease gene expression.Microbiological research · 2012Article
- Active role of the interdomain linker of AraC.Journal of bacteriology · 2011Article
- Unexpected coregulator range for the global regulator Lrp of Escherichia coli and Proteus mirabilis.Journal of bacteriology · 2011Article
- Regulation of arabinose and xylose metabolism in Escherichia coli.Applied and environmental microbiology · 2010Article
- A DNA-assisted binding assay for weak protein-protein interactions.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Escherichia coli AraC protein represses and induces the araBAD operon in response to the absence or presence of l-arabinose. Constitutive mutations in the AraC gene no longer require the presence of l-arabinose to convert AraC from its repressing to its inducing state. Such mutations were isolated directly by virtue of their constitutivity or by their resistance to the nonmetabolizable arabinose analog, d-fucose. The majority of the constitutive mutations lie within the same residues of the N-terminal regulatory arm of AraC. Two, however, were found in the core of the dimerization domain. As predicted by the light switch mechanism of AraC, constitutive mutations increase the susceptibility of the N-terminal arms to digestion by trypsin or chymotrypsin, suggesting that these mutations weaken or disrupt the arm structure required for repression by AraC. Fluorescence, circular dichroism, and cysteine reactivity measurements show that the constitutive mutations in the core of the dimerization domain lead to a weakening of the support for the arms and reduce the stability of the minus-arabinose arm structure. These mutations also weaken the interaction between the two-helix bundle and the beta-barrel subdomains of the dimerization domain and reduce the structural stability of the beta-barrels.
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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.