ArticleJournal of bacteriology2014
Charge requirements of lipid II flippase activity in Escherichia coli.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Structures of the lipid II flippase from the monoderm pathogen Staphylococcus aureus.The Journal of biological chemistry · 2026Article
- Mechanistic basis of teichoic acid transport by a gatekeeper flippase.Nature communications · 2026Article
- Article
- Proposed mechanism for Rft1-mediated scrambling of a dolichol-linked oligosaccharide.bioRxiv : the preprint server for biology · 2025Article
- Phage lysis protein LysScience advances · 2025Article
- Article
- Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022Review
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- Detection of Transport Intermediates in the Peptidoglycan Flippase MurJ Identifies Residues Essential for Conformational Cycling.Journal of the American Chemical Society · 2020Article
- Probing Conformational States of a Target Protein inBio-protocol · 2019Article
- Visualizing conformation transitions of the Lipid II flippase MurJ.Nature communications · 2019Article
- The bacterial lipid II flippase MurJ functions by an alternating-access mechanism.The Journal of biological chemistry · 2019Article
- Structure and mutagenic analysis of the lipid II flippase MurJ fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- A viral protein antibiotic inhibits lipid II flippase activity.Nature microbiology · 2017Article
- Crystal structure of the MOP flippase MurJ in an inward-facing conformation.Nature structural & molecular biology · 2017Article
- Filling holes in peptidoglycan biogenesis of Escherichia coli.Current opinion in microbiology · 2016Review
- The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences.Antibiotics (Basel, Switzerland) · 2016Article
- The O-Antigen Flippase Wzk Can Substitute for MurJ in Peptidoglycan Synthesis in Helicobacter pylori and Escherichia coli.PloS one · 2016Article
- LipidII: Just Another Brick in the Wall?PLoS pathogens · 2015Review
- Core Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and Opportunities.Antibiotics (Basel, Switzerland) · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Peptidoglycan (PG) is an extracytoplasmic glycopeptide matrix essential for the integrity of the envelope of most bacteria. The PG building block is a disaccharide-pentapeptide that is synthesized as a lipid-linked precursor called lipid II. The translocation of the amphipathic lipid II across the cytoplasmic membrane is required for subsequent incorporation of the disaccharide-pentapeptide into PG. In Escherichia coli, the essential inner membrane protein MurJ is the lipid II flippase. Previous studies showed that 8 charged residues in the central cavity region of MurJ are crucial for function. Here, we completed the functional analysis of all 57 charged residues in MurJ and demonstrated that the respective positive or negative charge of the 8 aforementioned residues is required for proper MurJ function. Loss of the negative charge in one of these residues, D39, causes a severe defect in MurJ biogenesis; by engineering an intragenic suppressor mutation that restores MurJ biogenesis, we found that this charge is also essential for MurJ function. Because of the low level of homology between MurJ and putative orthologs from Gram-positive bacteria, we explored the conservation of these 8 charged residues in YtgP, a homolog from Streptococcus pyogenes. We found that only 3 positive charges are similarly positioned and essential in YtgP; YtgP possesses additional charged residues within its predicted cavity that are essential for function and conserved among Gram-positive bacteria. From these data, we hypothesize that some charged residues in the cavity region of MurJ homologs are required for interaction with lipid II and/or energy coupling during transport.
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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.