ArticleNucleic acids research2022
Molecular basis for cell-wall recycling regulation by transcriptional repressor MurR in Escherichia coli.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Mechanism of NanR transcriptional activation of sialic acid metabolism in Streptococcus pneumoniae.Nucleic acids research · 2026Article
- Multilevel Regulation of Peptidoglycan Dynamics in Bacteria: From Molecular Mechanisms to Applied Perspectives.Biomolecules · 2026Review
- A small RNA fromVirulence · 2025Article
- Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025Review
- Molecular mechanism of the one-component regulator RccR on bacterial metabolism and virulence.Nucleic acids research · 2024Article
- BacPE: a versatile prime-editing platform in bacteria by inhibiting DNA exonucleases.Nature communications · 2024Article
- RegulonDB v12.0: a comprehensive resource of transcriptional regulation in E. coli K-12.Nucleic acids research · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell-wall recycling process is important for bacterial survival in nutrient-limited conditions and, in certain cases, is directly involved in antibiotic resistance. In the sophisticated cell-wall recycling process in Escherichia coli, the transcriptional repressor MurR controls the expression of murP and murQ, which are involved in transporting and metabolizing N-acetylmuramic acid (MurNAc), generating N-acetylmuramic acid-6-phosphate (MurNAc-6-P) and N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Here, we report that both MurNAc-6-P and GlcNAc-6-P can bind to MurR and weaken the DNA binding ability of MurR. Structural characterizations of MurR in complex with MurNAc-6-P or GlcNAc-6-P as well as in the apo form revealed the detailed ligand recognition chemistries. Further studies showed that only MurNAc-6-P, but not GlcNAc-6-P, is capable of derepressing the expression of murQP controlled by MurR in cells and clarified the substrate specificity through the identification of key residues responsible for ligand binding in the complex structures. In summary, this study deciphered the molecular mechanism of the cell wall recycling process regulated by MurR in E. coli.
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