ArticleProceedings of the National Academy of Sciences of the United States of America2015
Thermodynamic mechanism for inhibition of lactose permease by the phosphotransferase protein IIAGlc.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Strategies and applications for alleviating carbon catabolite repression.Synthetic and systems biotechnology · 2027Review
- From biophysical interaction to structural modeling: bi-terminal G and TGS domains drive rice OsYchF1-OsGAP1 complex formation.Botanical studies · 2025Article
- Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mobile barrier mechanisms for NaeLife · 2024Article
- Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023Article
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Preference of Bacterial Rhamnosyltransferases for 6-Deoxysugars Reveals a Strategy To Deplete O-Antigens.Journal of the American Chemical Society · 2023Article
- Article
- Inducer exclusion, by itself, cannot account for the glucose-mediated lac repression of Escherichia coli.Biophysical journal · 2022Article
- Cooperative binding ensures the obligatory melibiose/Na+ cotransport in MelB.The Journal of general physiology · 2021Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Thermodynamic insights into an interaction between ACYL-CoA-BINDING PROTEIN2 and LYSOPHOSPHOLIPASE2 inThe Journal of biological chemistry · 2019Article
- Regulation of metabolism in Escherichia coli during growth on mixtures of the non-glucose sugars: arabinose, lactose, and xylose.Scientific reports · 2018Article
- Contributions of SpoT Hydrolase, SpoT Synthetase, and RelA Synthetase to Carbon Source Diauxic Growth Transitions inFrontiers in microbiology · 2018Article
- Thermodynamic cooperativity of cosubstrate binding and cation selectivity ofThe Journal of general physiology · 2017Article
- Variable-Internal-Stores models of microbial growth and metabolism with dynamic allocation of cellular resources.Journal of mathematical biology · 2017Article
- Thermodynamics of Nanobody Binding to Lactose Permease.Biochemistry · 2016Article
- Effect of Detergents on Galactoside Binding by Melibiose Permeases.Biochemistry · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
In a variety of bacteria, the phosphotransferase protein IIA(Glc) plays a key regulatory role in catabolite repression in addition to its role in the vectorial phosphorylation of glucose catalyzed by the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). The lactose permease (LacY) of Escherichia coli catalyzes stoichiometric symport of a galactoside with an H(+), using a mechanism in which sugar- and H(+)-binding sites become alternatively accessible to either side of the membrane. Both the expression (via regulation of cAMP levels) and the activity of LacY are subject to regulation by IIA(Glc) (inducer exclusion). Here we report the thermodynamic features of the IIA(Glc)-LacY interaction as measured by isothermal titration calorimetry (ITC). The studies show that IIA(Glc) binds to LacY with a Kd of about 5 μM and a stoichiometry of unity and that binding is driven by solvation entropy and opposed by enthalpy. Upon IIA(Glc) binding, the conformational entropy of LacY is restrained, which leads to a significant decrease in sugar affinity. By suppressing conformational dynamics, IIA(Glc) blocks inducer entry into cells and favors constitutive glucose uptake and utilization. Furthermore, the studies support the notion that sugar binding involves an induced-fit mechanism that is inhibited by IIA(Glc) binding. The precise mechanism of the inhibition of LacY by IIA(Glc) elucidated by ITC differs from the inhibition of melibiose permease (MelB), supporting the idea that permeases can differ in their thermodynamic response to binding IIA(Glc).
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