ArticleJournal of the American Chemical Society2019
Direction of Chain Growth and Substrate Preferences of Shape, Elongation, Division, and Sporulation-Family Peptidoglycan Glycosyltransferases.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- RodA promotes intestinal colonization by group BInfection and immunity · 2026Article
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- Phage protein Gp11 blocksmBio · 2024Article
- Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.Nature communications · 2023Article
- CsbD, a Novel Group B Streptococcal Stress Response Factor That Contributes to Bacterial Resistance against Environmental Bile Salts.Journal of bacteriology · 2023Article
- A Time-Resolved FRET Assay Identifies a Small Molecule that Inhibits the Essential Bacterial Cell Wall Polymerase FtsW.Angewandte Chemie (International ed. in English) · 2023Article
- Recent Advances in Peptidoglycan Synthesis and Regulation in Bacteria.Biomolecules · 2023Review
- Masters of Misdirection: Peptidoglycan Glycosidases in Bacterial Growth.Journal of bacteriology · 2023Review
- Inhibition ofMicrobiology (Reading, England) · 2022Article
- Identification of the potential active site of the septal peptidoglycan polymerase FtsW.PLoS genetics · 2022Article
- Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Integrative structural biology of the penicillin-binding protein-1 fromComputational and structural biotechnology journal · 2021Article
- Peptidoglycan: Structure, Synthesis, and Regulation.EcoSal Plus · 2021Article
- Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization.Nature microbiology · 2021Article
- Regulation of peptidoglycan synthesis and remodelling.Nature reviews. Microbiology · 2020Review
- Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes.The Journal of biological chemistry · 2020Review
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial cell wall is composed of peptidoglycan, and its biosynthesis is an established target for antibiotics. Peptidoglycan is assembled from a glycopeptide precursor, Lipid II, that is polymerized by peptidoglycan glycosyltransferases into glycan strands that are subsequently cross-linked to form the mature cell wall. For decades bacteria were thought to contain only one family of enzymes that polymerize Lipid II, but recently, the ubiquitous Shape, Elongation, Division, and Sporulation (SEDS)-family proteins RodA and FtsW were shown to be peptidoglycan polymerases. Because RodA and FtsW are essential in nearly all bacteria, these enzymes are promising targets for new antibiotics. However, almost nothing is known about the mechanisms of these polymerases. Here, we report that SEDS proteins synthesize peptidoglycan by adding new Lipid II monomers to the reducing end of the growing glycan chain. Using substrates that can only react at the reducing end, we also show that the glycosyl donor and acceptor in the polymerization reaction have distinct lipid requirements. These findings provide the first fundamental insights into the mechanism of SEDS-family polymerases and lay the groundwork for future biochemical and structural studies.
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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.