ArticleThe Journal of biological chemistry2015
The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Harnessing prokaryotic amino acid transporters for metabolic engineering: mechanisms and biotechnological applications.Synthetic and systems biotechnology · 2026Review
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Drug-dependent inhibition of nucleotide hydrolysis in the heterodimeric ABC multidrug transporter PatAB from Streptococcus pneumoniae.The FEBS journal · 2022Article
- The Global Regulator PhoU Positively Controls Growth and Butenyl-Spinosyn Biosynthesis inFrontiers in microbiology · 2022Article
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- Cystine import is a valuable but risky process whose hazards Escherichia coli minimizes by inducing a cysteine exporter.Molecular microbiology · 2020Article
- Control of theEcoSal Plus · 2019Review
- Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanistic diversity in ATP-binding cassette (ABC) transporters.Nature structural & molecular biology · 2016Review
- The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex.Biological chemistry · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The MetNI methionine importer of Escherichia coli, an ATP binding cassette (ABC) transporter, uses the energy of ATP binding and hydrolysis to catalyze the high affinity uptake of D- and L-methionine. Early in vivo studies showed that the uptake of external methionine is repressed by the level of the internal methionine pool, a phenomenon termed transinhibition. Our understanding of the MetNI mechanism has thus far been limited to a series of crystal structures in an inward-facing conformation. To understand the molecular mechanism of transinhibition, we studied the kinetics of ATP hydrolysis using detergent-solubilized MetNI. We find that transinhibition is due to noncompetitive inhibition by L-methionine, much like a negative feedback loop. Thermodynamic analyses revealed two allosteric methionine binding sites per transporter. This quantitative analysis of transinhibition, the first to our knowledge for a structurally defined transporter, builds upon the previously proposed structurally based model for regulation. This mechanism of regulation at the transporter activity level could be applicable to not only ABC transporters but other types of membrane transporters as well.
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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.