ArticleProceedings of the National Academy of Sciences of the United States of America2011
Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 80 citations in OpenAlex.
- Microbial phosphorus cycling in terrestrial ecosystems.Nature reviews. Microbiology · 2026Review
- Metal-independent effects of calprotectin on cocultures ofbioRxiv : the preprint server for biology · 2026Article
- Predicting clinical outcome ofMicrobial genomics · 2025Article
- Physicochemistry and comparative metagenomics of a tropical estuary persistently inundated with anthropogenic pollutants.Folia microbiologica · 2025Article
- Phylogenetic analysis of microbial CP-lyase cluster genes for bioremediation of phosphonate.AMB Express · 2025Article
- Disentangling the Regulatory Response ofACS synthetic biology · 2024Article
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
- Epigenetic-Based Regulation of Transcriptome in Escherichia coli Adaptive Antibiotic Resistance.Microbiology spectrum · 2023Article
- Microbiomes and glyphosate biodegradation in edaphic and aquatic environments: recent issues and trends.World journal of microbiology & biotechnology · 2022Review
- Comparative Genomics Assisted Functional Characterization ofFrontiers in microbiology · 2022Article
- Dual transcriptomic analysis reveals metabolic changes associated with differential persistence of human pathogenic bacteria in leaves of Arabidopsis and lettuce.G3 (Bethesda, Md.) · 2021Article
- Genome Mining and Comparative Genome Analysis Revealed Niche-Specific Genome Expansion in AntibacterialGenes · 2021Article
- Expanding Characterized Diversity and the Pool of Complete Genome Sequences ofFrontiers in microbiology · 2021Article
- Gene Expansion and Positive Selection as Bacterial Adaptations to Oligotrophic Conditions.mSphere · 2019Article
- Inducible T7 RNA Polymerase-mediated Multigene Expression System, pMGX.Journal of visualized experiments : JoVE · 2017Article
- Article
- Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK.Structure (London, England : 1993) · 2016Article
- Article
- Subunit Interactions within the Carbon-Phosphorus Lyase Complex from Escherichia coli.Biochemistry · 2015Article
- Efflux as a glutaraldehyde resistance mechanism in Pseudomonas fluorescens and Pseudomonas aeruginosa biofilms.Antimicrobial agents and chemotherapy · 2015Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Organophosphonate utilization by Escherichia coli requires the 14 cistrons of the phnCDEFGHIJKLMNOP operon, of which the carbon-phosphorus lyase has been postulated to consist of the seven polypeptides specified by phnG to phnM. A 5,660-bp DNA fragment encompassing phnGHIJKLM is cloned, followed by expression in E. coli and purification of Phn-polypeptides. PhnG, PhnH, PhnI, PhnJ, and PhnK copurify as a protein complex by ion-exchange, size-exclusion, and affinity chromatography. The five polypeptides also comigrate in native-PAGE. Cross-linking of the purified protein complex reveals a close proximity of PhnG, PhnI, PhnJ, and PhnK, as these subunits disappear concomitant with the formation of large cross-linked protein complexes. Two molecular forms are identified, a major form of molecular mass of approximately 260 kDa, a minor form of approximately 640 kDa. The stoichiometry of the protein complex is suggested to be PhnG(4)H(2)I(2)J(2)K. Deletion of individual phn genes reveals that a strain harboring plasmid-borne phnGHIJ produces a protein complex consisting of PhnG, PhnH, PhnI, and PhnJ, whereas a strain harboring plasmid-borne phnGIJK produces a protein complex consisting of PhnG and PhnI. We conclude that phnGHIJK specify a soluble multisubunit protein complex essential for organophosphonate utilization.
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