ArticleThe Journal of biological chemistry2015
PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 88 citations in OpenAlex.
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- In Hyphomicrobium denitrificans Two Related Sulfane-Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses.Molecular microbiology · 2025Article
- Radical SAM Enzyme WprB Catalyzes Uniform Cross-Link Topology between Trp-C5 and Arg-Cγ on the Precursor Peptide.ACS chemical biology · 2025Article
- Detoxifying bacterial genes for deoxynivalenol epimerization confer durable resistance to Fusarium head blight in wheat.Plant biotechnology journal · 2024Article
- Genome-based identification of phosphate-solubilizing capacities of soil bacterial isolates.AMB Express · 2024Article
- Hydrogen-Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE.ACS central science · 2024Article
- Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023Review
- RaS-RiPPs in Streptococci and the Human Microbiome.ACS bio & med chem Au · 2022Review
- How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery.ACS bio & med chem Au · 2022Review
- Comparative genomics and analysis of the mechanism of PQQ overproduction in Methylobacterium.World journal of microbiology & biotechnology · 2021Article
- Biosynthesis and Heterologous Expression of Cacaoidin, the First Member of the Lanthidin Family of RiPPs.Antibiotics (Basel, Switzerland) · 2021Article
- Fine-tuning ethanol oxidation pathway enzymes and cofactor PQQ coordinates the conflict between fitness and acetic acid production by Acetobacter pasteurianus.Microbial biotechnology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone.Current opinion in chemical biology · 2020Review
- Biological pincer complexes.ChemCatChem · 2020Article
- Challenges and advances in genome mining of ribosomally synthesized and post-translationally modified peptides (RiPPs).Synthetic and systems biotechnology · 2020Review
- Article
- Matters of class: coming of age of class III and IV lanthipeptides.RSC chemical biology · 2020Review
- Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters inJournal of the American Chemical Society · 2020Article
- Improved Production of Pyrroloquinoline Quinone by Simultaneous Augmentation of Its Synthesis Gene Expression and Glucose Metabolism in Klebsiella pneumoniae.Current microbiology · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Pyrroloquinoline quinone (PQQ) is a product of a ribosomally synthesized and post-translationally modified pathway consisting of five conserved genes, pqqA-E. PqqE is a radical S-adenosylmethionine (RS) protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA. PqqD is a 10-kDa protein with an unknown function, but is essential for PQQ production. Recently, in Klebsiella pneumoniae (Kp), PqqD and PqqE were shown to interact; however, the stoichiometry and KD were not obtained. Here, we show that the PqqE and PqqD interaction transcends species, also occurring in Methylobacterium extorquens AM1 (Me). The stoichiometry of the MePqqD and MePqqE interaction is 1:1 and the KD, determined by surface plasmon resonance spectroscopy (SPR), was found to be ∼12 μm. Moreover, using SPR and isothermal calorimetry techniques, we establish for the first time that MePqqD binds MePqqA tightly (KD ∼200 nm). The formation of a ternary MePqqA-D-E complex was captured by native mass spectrometry and the KD for the MePqqAD-MePqqE interaction was found to be ∼5 μm. Finally, using a bioinformatic analysis, we found that PqqD orthologues are associated with the RS-SPASM family of proteins (subtilosin, pyrroloquinoline quinone, anaerobic sulfatase maturating enzyme, and mycofactocin), all of which modify either peptides or proteins. In conclusion, we propose that PqqD is a novel peptide chaperone and that PqqD orthologues may play a similar role in peptide modification pathways that use an RS-SPASM protein.
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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.