ArticleJournal of bacteriology2002
The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Structural basis for negative regulation of the Escherichia coli maltose system.Nature communications · 2023Article
- Sensory Systems and Transcriptional Regulation inFrontiers in bioengineering and biotechnology · 2022Review
- Evolutionary dynamics and structural consequences of de novo beneficial mutations and mutant lineages arising in a constant environment.BMC biology · 2021Article
- High-throughput mapping of the phage resistance landscape in E. coli.PLoS biology · 2020Article
- d-Amino Acids and Lactic Acid Bacteria.Microorganisms · 2019Review
- A Novel Bifunctional Amino Acid Racemase With Multiple Substrate Specificity, MalY FromFrontiers in microbiology · 2018Article
- How 'arm-twisting' by the inducer triggers activation of the MalT transcription factor, a typical signal transduction ATPase with numerous domains (STAND).Nucleic acids research · 2015Article
- The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate.Molecular microbiology · 2012Article
- Constitutive expression of the maltoporin LamB in the absence of OmpR damages the cell envelope.Journal of bacteriology · 2011Article
- Exposure to Glycolytic Carbon Sources Reveals a Novel Layer of Regulation for the MalT Regulon.International journal of microbiology · 2011Article
- Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli.Journal of bacteriology · 2010Article
- Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.EcoSal Plus · 2010Article
- Bacterial adaptation through distributed sensing of metabolic fluxes.Molecular systems biology · 2010Article
- aes, the gene encoding the esterase B in Escherichia coli, is a powerful phylogenetic marker of the species.BMC microbiology · 2009Article
- E Unibus Plurum: genomic analysis of an experimentally evolved polymorphism in Escherichia coli.PLoS genetics · 2009Article
- A critical process controlled by MalT and OmpR is revealed through synthetic lethality.Journal of bacteriology · 2009Article
- Glucose- and glucokinase-controlled mal gene expression in Escherichia coli.Journal of bacteriology · 2009Article
- Parallel changes in global protein profiles during long-term experimental evolution in Escherichia coli.Genetics · 2006Article
- Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.Journal of bacteriology · 2005Article
- Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR.The EMBO journal · 2005Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maltose system of Escherichia coli consists of a number of genes encoding proteins involved in the uptake and metabolism of maltose and maltodextrins. The system is positively regulated by MalT, its transcriptional activator. MalT activity is controlled by two regulatory circuits: a positive one with maltotriose as effector and a negative one involving several proteins. MalK, the ATP-hydrolyzing subunit of the cognate ABC transporter, MalY, an enzyme with the activity of a cystathionase, and Aes, an acetyl esterase, phenotypically act as repressors of MalT activity. By in vivo titration assays, we have shown that the N-terminal 250 amino acids of MalT contain the interaction site for MalY but not for MalK. This was confirmed by gel filtration analysis, where MalY was shown to coelute with the N-terminal MalT structural domain. Mutants in MalT causing elevated mal gene expression in the absence of exogenous maltodextrins were tested in their response to the three repressors. The different MalT mutations exhibited a various degree of sensitivity towards these repressors, but none was resistant to all of them. Some of them became nearly completely resistant to Aes while still being sensitive to MalY. These mutations are located at positions 38, 220, 243, and 359, most likely defining the interaction patch with Aes on the three-dimensional structure of MalT.
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