ArticleScientific reports2020
The essential inner membrane protein YejM is a metalloenzyme.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Enteric-colonizedGut microbes · 2026Article
- Control of the committed step in lipopolysaccharide biosynthesis.The Journal of biological chemistry · 2026Review
- Membrane lipid homeostasis dually regulates conformational transition of phosphoethanolamine transferase EptA.Nature communications · 2024Article
- Article
- Distribution of virulence-associated genes, antibiotic resistance and phylogenetic groups in Escherichia coli isolated from domestic and racing pigeons.Veterinary research communications · 2023Article
- Retrospective analysis of drug resistance characteristics and infection related risk factors of multidrug-resistant organisms (MDROs) isolated from the orthopedics department of a tertiary hospital.Scientific reports · 2023Article
- Article
- Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality inInternational journal of molecular sciences · 2021Review
- The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner.Journal of microbiology (Seoul, Korea) · 2021Article
- Effect of Food Endotoxin on Infant Health.Toxins · 2021Review
- Comparison of Antimicrobial Resistance, Virulence Genes, Phylogroups, and Biofilm Formation ofFrontiers in microbiology · 2021Article
- Regulation of the First Committed Step in Lipopolysaccharide Biosynthesis Catalyzed by LpxC Requires the Essential Protein LapC (YejM) and HslVU Protease.International journal of molecular sciences · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent recurrent outbreaks of Gram-negative bacteria show the critical need to target essential bacterial mechanisms to fight the increase of antibiotic resistance. Pathogenic Gram-negative bacteria have developed several strategies to protect themselves against the host immune response and antibiotics. One such strategy is to remodel the outer membrane where several genes are involved. yejM was discovered as an essential gene in E. coli and S. typhimurium that plays a critical role in their virulence by changing the outer membrane permeability. How the inner membrane protein YejM with its periplasmic domain changes membrane properties remains unknown. Despite overwhelming structural similarity between the periplasmic domains of two YejM homologues with hydrolases like arylsulfatases, no enzymatic activity has been previously reported for YejM. Our studies reveal an intact active site with bound metal ions in the structure of YejM periplasmic domain. Furthermore, we show that YejM has a phosphatase activity that is dependent on the presence of magnesium ions and is linked to its function of regulating outer membrane properties. Understanding the molecular mechanism by which YejM is involved in outer membrane remodeling will help to identify a new drug target in the fight against the increased antibiotic resistance.
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