ArticleNucleic acids research2008
Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 74 citations in OpenAlex.
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- DipR, a GntR/FadR-family transcriptional repressor: regulatory mechanism and widespread distribution of the dip cluster for dipicolinic acid catabolism in bacteria.Nucleic acids research · 2024Article
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- Development of an miRFP680-Based Fluorescent Calcium Ion Biosensor Using End-Optimized Transposons.ACS sensors · 2024Article
- High-Performance Genetically Encoded Green Fluorescent Biosensors for Intracellular l-Lactate.ACS central science · 2024Article
- PcaR, a GntR/FadR Family Transcriptional Repressor Controls the Transcription of Phenazine-1-Carboxylic Acid 1,2-Dioxygenase Gene Cluster in Sphingomonas histidinilytica DS-9.Applied and environmental microbiology · 2023Article
- Revealing the Characteristics of Glucose- and Lactate-Based Chain Elongation for Caproate Production bymSystems · 2022Article
- Identification and characterization of L- and D-lactate-inducible systems from Escherichia coli MG1655, Cupriavidus necator H16 and Pseudomonas species.Scientific reports · 2022Article
- Transcription factor allosteric regulation through substrate coordination to zinc.NAR genomics and bioinformatics · 2021Article
- Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism.Nature communications · 2021Article
- Molecular Cloning, Purification and Characterization of Mce1R of Mycobacterium tuberculosis.Molecular biotechnology · 2021Article
- Characterization of the first tetrameric transcription factor of the GntR superfamily with allosteric regulation from the bacterial pathogen Agrobacterium fabrum.Nucleic acids research · 2021Article
- Key Enzymes for Anaerobic Lactate Metabolism in Geobacter sulfurreducens.Applied and environmental microbiology · 2021Article
- Structural and Functional Analyses of the Transcription Repressor DgoR FromFrontiers in microbiology · 2020Article
- Relevance of NADH Dehydrogenase and Alternative Two-Enzyme Systems for Growth ofFrontiers in bioengineering and biotechnology · 2020Article
- Elucidating the Role and Regulation of a Lactate Permease as Lactate Transporter in Bacillus coagulans DSM1.Applied and environmental microbiology · 2019Article
- Molecular and Functional Insights into the Regulation of d-Galactonate Metabolism by the Transcriptional Regulator DgoR inJournal of bacteriology · 2019Article
- Whole-cell Escherichia coli lactate biosensor for monitoring mammalian cell cultures during biopharmaceutical production.Biotechnology and bioengineering · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LldR (CGL2915) from Corynebacterium glutamicum is a transcription factor belonging to the GntR family, which is typically involved in the regulation of oxidized substrates associated with amino acid metabolism. In the present study, the crystal structure of LldR was determined at 2.05-A resolution. The structure consists of N- and C-domains similar to those of FadR, but with distinct domain orientations. LldR and FadR dimers achieve similar structures by domain swapping, which was first observed in dimeric assembly of transcription factors. A structural feature of Zn(2+) binding in the regulatory domain was also observed, as a difference from the FadR subfamily. DNA microarray and DNase I footprint analyses suggested that LldR acts as a repressor regulating cgl2917-lldD and cgl1934-fruK-ptsF operons, which are indispensable for l-lactate and fructose/sucrose utilization, respectively. Furthermore, the stoichiometries and affinities of LldR and DNAs were determined by isothermal titration calorimetry measurements. The transcriptional start site and repression of LldR on the cgl2917-lldD operon were analysed by primer extension assay. Mutation experiments showed that residues Lys4, Arg32, Arg42 and Gly63 are crucial for DNA binding. The location of the putative ligand binding cavity and the regulatory mechanism of LldR on its affinity for DNA were proposed.
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