ArticleJournal of bacteriology2012
The chbG gene of the chitobiose (chb) operon of Escherichia coli encodes a chitooligosaccharide deacetylase.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 40 citations in OpenAlex.
- Computational identification of multi-target natural compounds from Sesbania grandiflora as potential therapeutic agents against Klebsiella pneumoniae.Scientific reports · 2026Article
- YDJC restrains Th1 cell differentiation by blocking SREBP2-mediated cholesterol biosynthesis to alleviate mucosal inflammation in inflammatory bowel disease.Cellular & molecular immunology · 2026Article
- Genomic diversity in Paenibacillus polymyxa: unveiling distinct species groups and functional variability.BMC genomics · 2024Article
- Crystal structure of ChbG from Klebsiella pneumoniae reveals the molecular basis of diacetylchitobiose deacetylation.Communications biology · 2022Article
- Customized chitooligosaccharide production-controlling their lengthFrontiers in bioengineering and biotechnology · 2022Article
- A bottom-up approach towards a bacterial consortium for the biotechnological conversion of chitin to L-lysine.Applied microbiology and biotechnology · 2021Article
- Identification and Characterization of a β-International journal of molecular sciences · 2020Article
- Review
- YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A.Journal of oncology · 2019Article
- YdjC chitooligosaccharide deacetylase homolog induces keratin reorganization in lung cancer cells: involvement of interaction between YDJC and CDC16.Oncotarget · 2018Article
- Review
- Functional analysis of an unusual porin-like channel that imports chitin for alternative carbon metabolism inThe Journal of biological chemistry · 2017Article
- Article
- Identification and Functional Characterization of a Novel OprD-like Chitin Uptake Channel in Non-chitinolytic Bacteria.The Journal of biological chemistry · 2016Article
- One-carbon metabolic pathway rewiring in Escherichia coli reveals an evolutionary advantage of 10-formyltetrahydrofolate synthetase (Fhs) in survival under hypoxia.Journal of bacteriology · 2015Article
- Overexpression of an outer membrane protein associated with decreased susceptibility to carbapenems in Proteus mirabilis.PloS one · 2015Article
- N-acetylglucosamine (GlcNAc) functions in cell signaling.Scientifica · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chb operon of Escherichia coli is involved in the utilization of the β-glucosides chitobiose and cellobiose. The function of chbG (ydjC), the sixth open reading frame of the operon that codes for an evolutionarily conserved protein is unknown. We show that chbG encodes a monodeacetylase that is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. The predicted active site of the enzyme was validated by demonstrating loss of function upon substitution of its putative metal-binding residues that are conserved across the YdjC family of proteins. We show that activation of the chb promoter by the regulatory protein ChbR is dependent on ChbG, suggesting that deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for their recognition by ChbR as inducers. Strains carrying mutations in chbR conferring the ability to grow on both cellobiose and chitobiose are independent of chbG function for induction, suggesting that gain of function mutations in ChbR allow it to recognize the acetylated form of the oligosaccharides. ChbR-independent expression of the permease and phospho-β-glucosidase from a heterologous promoter did not support growth on both chitobiose and chitotriose in the absence of chbG, suggesting an additional role of chbG in the hydrolysis of chitooligosaccharides. The homologs of chbG in metazoans have been implicated in development and inflammatory diseases of the intestine, indicating that understanding the function of E. coli chbG has a broader significance.
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