ArticleNucleic acids research2013
Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domain.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Pathway remodeling and adaptive evolution enable efficient co-utilization of glucose and xylose inmBio · 2026Article
- Complete xylan utilization pathway and regulation mechanisms involved in marine algae degradation by cosmopolitan marine and human gut microbiota.The ISME journal · 2025Article
- XylR regulates genes at xyl cluster, involved in D-xylose catabolism in Herbaspirillum seropedicae Z69.Archives of microbiology · 2024Article
- Investigating and Engineering an 1,2-Propanediol-Responsive Transcription Factor-Based Biosensor.ACS synthetic biology · 2024Article
- Article
- Synthetic Gene Circuits for Regulation of Next-Generation Cell-Based Therapeutics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- D-Xylose Blocks the Broad Negative Regulation of XylR on Lipid Metabolism and Affects Multiple Physiological Characteristics in Mycobacteria.International journal of molecular sciences · 2023Article
- Determination of Mutational Timing of Colistin-Resistance Genes throughPharmaceutics · 2023Article
- Diversity in Genetic Regulation of Bacterial Fimbriae Assembled by the Chaperone Usher Pathway.International journal of molecular sciences · 2022Review
- Regulation of Transgene Expression by the Natural Sweetener Xylose.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- A mouse model of occult intestinal colonization demonstrating antibiotic-induced outgrowth of carbapenem-resistant Enterobacteriaceae.Microbiome · 2022Article
- Efficient anaerobic consumption of D-xylose by E. coli BL21(DE3) via xylR adaptive mutation.BMC microbiology · 2021Article
- D-Xylose Sensing inInternational journal of molecular sciences · 2021Review
- Optimised Heterologous Expression and Functional Analysis of theInternational journal of molecular sciences · 2021Article
- Unraveling the role of the transcriptional regulator VirS in low pH-induced responses ofThe Journal of biological chemistry · 2019Article
- Functional Mechanism of the Efflux Pumps Transcription Regulators FromFrontiers in molecular biosciences · 2018Review
- Experimental evolution reveals an effective avenue to release catabolite repression via mutations in XylR.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A large family of anti-activators accompanying XylS/AraC family regulatory proteins.Molecular microbiology · 2016Article
- AutA and AutR, Two Novel Global Transcriptional Regulators, Facilitate Avian Pathogenic Escherichia coli Infection.Scientific reports · 2016Article
- Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
Escherichia coli can rapidly switch to the metabolism of l-arabinose and d-xylose in the absence of its preferred carbon source, glucose, in a process called carbon catabolite repression. Transcription of the genes required for l-arabinose and d-xylose consumption is regulated by the sugar-responsive transcription factors, AraC and XylR. E. coli represents a promising candidate for biofuel production through the metabolism of hemicellulose, which is composed of d-xylose and l-arabinose. Understanding the l-arabinose/d-xylose regulatory network is key for such biocatalyst development. Unlike AraC, which is a well-studied protein, little is known about XylR. To gain insight into XylR function, we performed biochemical and structural studies. XylR contains a C-terminal AraC-like domain. However, its N-terminal d-xylose-binding domain contains a periplasmic-binding protein (PBP) fold with structural homology to LacI/GalR transcription regulators. Like LacI/GalR proteins, the XylR PBP domain mediates dimerization. However, unlike LacI/GalR proteins, which dimerize in a parallel, side-to-side manner, XylR PBP dimers are antiparallel. Strikingly, d-xylose binding to this domain results in a helix to strand transition at the dimer interface that reorients both DNA-binding domains, allowing them to bind and loop distant operator sites. Thus, the combined data reveal the ligand-induced activation mechanism of a new family of DNA-binding proteins.
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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.