ArticleGlycobiology2014
A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability.
Article in Glycobiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Cofitness network connectivity determines a fuzzy essential zone in open bacterial pangenome.mLife · 2024Article
- Heterogenous Expression and Purification of Lipid II Flippase fromProtein and peptide letters · 2024Article
- 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
- Improved Dynamic Range of a Rhamnose-Inducible Promoter for Gene Expression inApplied and environmental microbiology · 2021Article
- Bacterial nanotubes as a manifestation of cell death.Nature communications · 2020Article
- The bacterial lipid II flippase MurJ functions by an alternating-access mechanism.The Journal of biological chemistry · 2019Article
- Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018Review
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
- Comparative analysis of the Burkholderia cenocepacia K56-2 essential genome reveals cell envelope functions that are uniquely required for survival in species of the genus Burkholderia.Microbial genomics · 2017Article
- Crystal structure of the MOP flippase MurJ in an inward-facing conformation.Nature structural & molecular biology · 2017Article
- The Escherichia coli rhaSR-PrhaBAD Inducible Promoter System Allows Tightly Controlled Gene Expression over a Wide Range in Pseudomonas aeruginosa.Applied and environmental microbiology · 2016Article
- Candidate Essential Genes in Burkholderia cenocepacia J2315 Identified by Genome-Wide TraDIS.Frontiers in microbiology · 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
- The Mycobacterial Cell Wall--Peptidoglycan and Arabinogalactan.Cold Spring Harbor perspectives in medicine · 2015Review
- Lipid Flippases for Bacterial Peptidoglycan Biosynthesis.Lipid insights · 2015Review
- Charge requirements of lipid II flippase activity in Escherichia coli.Journal of bacteriology · 2014Article
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Authors and funding
2 authors at 2 institutions in 3 countries.
Funding
Abstract
The cell wall peptidoglycan (PG) of Burkholderia cenocepacia, an opportunistic pathogen, has not yet been characterized. However, the B. cenocepacia genome contains homologs of genes encoding PG biosynthetic functions in other bacteria. PG biosynthesis involves the formation of the undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide, known as lipid II, which is built on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh; this translocation step is critical to PG synthesis. We have investigated candidate flippase homologs of the MurJ family in B. cenocepacia. Our results show that BCAL2764, herein referred to as murJBc, is indispensable for viability. Viable B. cenocepacia could only be obtained through a conditional mutagenesis strategy by placing murJBc under the control of a rhamnose-inducible promoter. Under rhamnose depletion, the conditional strain stopped growing and individual cells displayed morphological abnormalities consistent with a defect in PG synthesis. Bacterial cells unable to express MurJBc underwent cell lysis, while partial MurJBc depletion sensitized the mutant to the action of β-lactam antibiotics. Depletion of MurJBc caused accumulation of PG precursors consistent with the notion that this protein plays a role in lipid II flipping to the periplasmic compartment. Reciprocal complementation experiments of conditional murJ mutants in B. cenocepacia and Escherichia coli with plasmids expressing MurJ from each strain indicated that MurJBc and MurJEc are functional homologs. Together, our results are consistent with the notion that MurJBc is a PG lipid II flippase in B. cenocepacia.
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