ArticleJournal of bacteriology2005
The gusBC genes of Escherichia coli encode a glucuronide transport system.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 61 citations in OpenAlex.
- Structure-based classification of bacterial chitooligosaccharide-specific outer membrane porins (ChiPs).The Journal of biological chemistry · 2026Article
- In vitro inhibition of Escherichia coli β-glucuronidase by aripiprazole.Pharmacological reports : PR · 2026Article
- EefR mutations drive sanguinarine resistance by activating cryptic multidrug efflux pumps in AcrB-NullVirulence · 2025Article
- Patterns of Fitness and Gene Expression Epistasis Generated by Beneficial Mutations in the rho and rpoB Genes of Escherichia coli during High-Temperature Adaptation.Molecular biology and evolution · 2024Article
- Orally Administered Drugs and Their Complicated Relationship with Our Gastrointestinal Tract.Microorganisms · 2024Review
- Paradoxical Activation of a Type VI Secretion System Phospholipase Effector by Its Cognate Immunity Protein.Journal of bacteriology · 2023Article
- Metabolically-targeted dCas9 expression in bacteria.Nucleic acids research · 2023Article
- Proteomes of UropathogenicProteomes · 2022Article
- Unveiling the Virulent Genotype and Unusual Biochemical Behavior of Escherichia coli ST59.Applied and environmental microbiology · 2021Article
- Article
- First Occurrence of the OXA-198 Carbapenemase inAntimicrobial agents and chemotherapy · 2020Article
- Rapid Detection of Escherichia coli in Water Using Sample Concentration and Optimized Enzymatic Hydrolysis of Chromogenic Substrates.Current microbiology · 2018Article
- Structural basis for the regulation of β-glucuronidase expression by human gut Enterobacteriaceae.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- An Atlas of β-Glucuronidases in the Human Intestinal Microbiome.Structure (London, England : 1993) · 2017Article
- Real-time imaging of intestinal bacterial β-glucuronidase activity by hydrolysis of a fluorescent probe.Scientific reports · 2017Article
- Computational Analysis of Host-Pathogen Protein Interactions between Humans and Different Strains of EnterohemorrhagicFrontiers in cellular and infection microbiology · 2017Article
- MDSINE: Microbial Dynamical Systems INference Engine for microbiome time-series analyses.Genome biology · 2016Article
- Fluorescence assay for evaluating microbicidal activity of hand antiseptics.Applied and environmental microbiology · 2015Article
- Impediments to enhancement of CPT-11 anticancer activity by E. coli directed beta-glucuronidase therapy.PloS one · 2015Article
- Two-dimensional crystalline array formation of glucuronide transporter from Escherichia coli by the use of polystyrene beads for detergent removal.The Journal of membrane biology · 2013Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes, gusB and gusC, from a natural fecal isolate of Escherichia coli are shown to encode proteins responsible for transport of beta-glucuronides with synthetic [(14)C]phenyl-1-thio-beta-d-glucuronide as the substrate. These genes are located in the gus operon downstream of the gusA gene on the E. coli genome, and their expression is induced by a variety of beta-d-glucuronides. Measurements of transport in right-side-out subcellular vesicles show the system has the characteristics of secondary active transport energized by the respiration-generated proton motive force. When the genes were cloned together downstream of the tac operator-promoter in the plasmid pTTQ18 expression vector, transport activity was increased considerably with isopropylthiogalactopyranoside as the inducer. Amplified expression of the GusB and GusC proteins enabled visualization and identification by N-terminal sequencing of both proteins, which migrated at ca. 32 kDa and 44 kDa, respectively. Separate expression of the GusB protein showed that it is essential for glucuronide transport and is located in the inner membrane, while the GusC protein does not catalyze transport but assists in an as yet unknown manner and is located in the outer membrane. The output of glucuronides as waste by mammals and uptake for nutrition by gut bacteria or reabsorption by the mammalian host is discussed.
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