ArticleJournal of bacteriology2009
Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence for GTP cyclohydrolase IB.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
54 citing papers in PubMed, 79 citations in OpenAlex.
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- How mutagenesis and laboratory conditions affect the genome of the metal-resistant bacteriumJournal of bacteriology · 2026Article
- The β-lactam adjuvant guanosine potentiates anti-folate antibiotics and pyrimidine synthesis inhibitors by depleting thymidine in methicillin-resistantbioRxiv : the preprint server for biology · 2026Article
- The adaptation chip: repurposing the principles of the ichip for guiding in situ experimental evolution.ISME communications · 2026Article
- Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025Review
- Multi-faceted exploration of the novel active γ-carbonic anhydrase PaCAγ1 in the human pathogen Pseudomonas aeruginosa.International journal of biological macromolecules · 2025Article
- Reductive activation of the disulfide-containing antibiotic thiolutin is mediated by both bacillithiol and FAD-dependent disulfide reductases.Journal of bacteriology · 2025Article
- Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion.ACS catalysis · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- The Leptospira interrogans proteome's response to zinc highlights the potential involvement of this metal in translational-machinery and virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- The efflux system CdfX exports zinc that cannot be transported by ZntA inJournal of bacteriology · 2024Article
- Combatting melioidosis with chemical synthetic lethality.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The metal-binding GTPases CobW2 and CobW3 are at the crossroads of zinc and cobalt homeostasis inJournal of bacteriology · 2024Article
- Microbes vary strategically in their metalation of mononuclear enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages.Microbiology and molecular biology reviews : MMBR · 2024Review
- Protecting the Achilles heel: three FolE_I-type GTP-cyclohydrolases needed for full growth of metal-resistantJournal of bacteriology · 2024Article
- Article
- The elements of life: A biocentric tour of the periodic table.Advances in microbial physiology · 2023Article
- Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- As(III) Exposure Induces a Zinc Scarcity Response and Restricts Iron Uptake in High-Level Arsenic-Resistant Paenibacillus taichungensis Strain NC1.Applied and environmental microbiology · 2022Article
Corrections and comments
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Authors and funding
11 authors at 7 institutions in 1 country.
Funding
Abstract
GTP cyclohydrolase I (GCYH-I) is an essential Zn(2+)-dependent enzyme that catalyzes the first step of the de novo folate biosynthetic pathway in bacteria and plants, the 7-deazapurine biosynthetic pathway in Bacteria and Archaea, and the biopterin pathway in mammals. We recently reported the discovery of a new prokaryotic-specific GCYH-I (GCYH-IB) that displays no sequence identity to the canonical enzyme and is present in approximately 25% of bacteria, the majority of which lack the canonical GCYH-I (renamed GCYH-IA). Genomic and genetic analyses indicate that in those organisms possessing both enzymes, e.g., Bacillus subtilis, GCYH-IA and -IB are functionally redundant, but differentially expressed. Whereas GCYH-IA is constitutively expressed, GCYH-IB is expressed only under Zn(2+)-limiting conditions. These observations are consistent with the hypothesis that GCYH-IB functions to allow folate biosynthesis during Zn(2+) starvation. Here, we present biochemical and structural data showing that bacterial GCYH-IB, like GCYH-IA, belongs to the tunneling-fold (T-fold) superfamily. However, the GCYH-IA and -IB enzymes exhibit significant differences in global structure and active-site architecture. While GCYH-IA is a unimodular, homodecameric, Zn(2+)-dependent enzyme, GCYH-IB is a bimodular, homotetrameric enzyme activated by a variety of divalent cations. The structure of GCYH-IB and the broad metal dependence exhibited by this enzyme further underscore the mechanistic plasticity that is emerging for the T-fold superfamily. Notably, while humans possess the canonical GCYH-IA enzyme, many clinically important human pathogens possess only the GCYH-IB enzyme, suggesting that this enzyme is a potential new molecular target for antibacterial development.
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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.