Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway

Jochimsen, Bjarne; Lolle, Signe; McSorley, Fern R.; Nabi, Mariah; Stougaard, Jens; Zechel, David L.; Hove‐Jensen, Bjarne

doi:10.1073/pnas.1104922108

Cited by 65 publications

(71 citation statements)

References 27 publications

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“…Additionally, these data are consistent with results obtained Ͼ2 decades ago by Frost and coworkers, who demonstrated that C-P bond cleavage by C-P lyase occurs by a radical reaction mechanism (44)(45)(46). Also, amino acid sequence alignments of Phn polypeptides revealed a remarkable evolutionary conservation of PhnJ compared to other Phn polypeptides, consistent with the critical enzymatic function of PhnJ (40,47). The 2-hydroxyl of the phosphoribosyl moiety plays a crucial role in C-P lyase catalysis, possibly in turning over a covalent PhnJ-phosphoribosyl intermediate.…”

Section: Mesorhizobium Lotisupporting

confidence: 80%

“…which may cause the coupling of transport and catabolism of phosphonic acids (40). Additionally, the phnGHIJK cistrons, i.e., the cistrons encoding the PhnGHIJK protein complex, show translational coupling.…”

Section: The Phosphonate Proteome and Transport Metabolonmentioning

confidence: 99%

“…3. A multisubunit protein complex, PhnGHIJK, was identified (40). No enzymatic activity of PhnGHIJK was demonstrated, but in vitro analysis has shown that PhnI has ribonucleoside 5=-triphosphate nucleosidase activity (ATP/ GTP ϩ H 2 O ¡ ribosyl 5-triphosphate ϩ adenine/guanine), whereas PhnI in the presence of PhnG, PhnH, and PhnL has ribonucleoside 5=-triphosphate phosphonylase activity (ATP/GTP ϩ methylphosphonic acid ¡ 5=-triphosphoribosyl 1=-methylphosphonate ϩ adenine/guanine) (EC 2.7. )…”

Section: Mesorhizobium Lotimentioning

confidence: 99%

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Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Hove‐Jensen

Zechel

Jochimsen

2014

Microbiol Mol Biol Rev

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181

157

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SUMMARY After several decades of use of glyphosate, the active ingredient in weed killers such as Roundup, in fields, forests, and gardens, the biochemical pathway of transformation of glyphosate phosphorus to a useful phosphorus source for microorganisms has been disclosed. Glyphosate is a member of a large group of chemicals, phosphonic acids or phosphonates, which are characterized by a carbon-phosphorus bond. This is in contrast to the general phosphorus compounds utilized and metabolized by microorganisms. Here phosphorus is found as phosphoric acid or phosphate ion, phosphoric acid esters, or phosphoric acid anhydrides. The latter compounds contain phosphorus that is bound only to oxygen. Hydrolytic, oxidative, and radical-based mechanisms for carbon-phosphorus bond cleavage have been described. This review deals with the radical-based mechanism employed by the carbon-phosphorus lyase of the carbon-phosphorus lyase pathway, which involves reactions for activation of phosphonate, carbon-phosphorus bond cleavage, and further chemical transformation before a useful phosphate ion is generated in a series of seven or eight enzyme-catalyzed reactions. The phn genes, encoding the enzymes for this pathway, are widespread among bacterial species. The processes are described with emphasis on glyphosate as a substrate. Additionally, the catabolism of glyphosate is intimately connected with that of aminomethylphosphonate, which is also treated in this review. Results of physiological and genetic analyses are combined with those of bioinformatics analyses.

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Section: Mesorhizobium Lotisupporting

confidence: 80%

Section: The Phosphonate Proteome and Transport Metabolonmentioning

confidence: 99%

Section: Mesorhizobium Lotimentioning

confidence: 99%

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Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Hove‐Jensen

Zechel

Jochimsen

2014

Microbiol Mol Biol Rev

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181

157

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“…Phosphonate-binding and -uptake proteins have not previously been described as playing a role in biofilm formation. In E. coli, phosphonates are taken into the cell and converted to phosphates, likely to meet nutritional requirements (30)(31)(32)(33). It is not known if PhnD has an analogous role in S. epidermidis.…”

Section: Discussionmentioning

confidence: 99%

Antibodies to PhnD Inhibit Staphylococcal Biofilms

et al. 2014

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Biofilm formation on central lines or peripheral catheters is a serious threat to patient well-being. Contaminated vascular devices can act as a nidus for bloodstream infection and systemic pathogen dissemination. Staphylococcal biofilms are the most common cause of central-line-associated bloodstream infections, and antibiotic resistance makes them difficult to treat. As an alternative to antibiotic intervention, we sought to identify anti-staphylococcal biofilm targets for the development of a vaccine or antibody prophylactic. A screening strategy was devised using a microfluidic system to test antibody-mediated biofilm inhibition under biologically relevant conditions of shear flow. Affinity-purified polyclonal antibodies to target antigen PhnD inhibited both Staphylococcus epidermidis and S. aureus biofilms. PhnD-specific antibodies blocked biofilm development at the initial attachment and aggregation stages, and deletion of phnD inhibited normal biofilm formation. We further adapted our microfluidic biofilm system to monitor the interaction of human neutrophils with staphylococcal biofilms and demonstrated that PhnD-specific antibodies also serve as opsonins to enhance neutrophil binding, motility, and biofilm engulfment. These data support the identification of PhnD as a lead target for biofilm intervention strategies performed either by vaccination or through passive administration of antibodies.

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“…The phnCDEFGHIJKLMNOP operon encodes 14 proteins essential for growth on phosphonates such as MePn: PhnE is the permease subunit in the PhnCDE ABC transporter, and PhnGHIJK form the complex essential for cleaving the C-P bond in phosphonates (15,26,35). We confirmed that the evolved strain ENZ1901 (phnE ϩ ) grew with the same efficiency on MePn or P i as the sole source of P, whereas the ancestral strain ENZ535 (phnE::8 bp) did not grow on MePn but gave rise to variants at a high frequency of Ϸ2 MePn ϩ cells per 10 5 total cells (data not shown), compared with a typical frequency of Ϸ10 Ϫ7 for a singlebase substitution (10).…”

Section: Figmentioning

confidence: 99%

Activation of the Cryptic PhnE Permease Promotes Rapid Adaptive Evolution in a Population of Escherichia coli K-12 Starved for Phosphate

Guillemet

Moreau

2012

J Bacteriol

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Escherichia coli K-12 suffers acetic acid stress during prolonged incubation in glucose minimal medium containing a limiting concentration of inorganic phosphate (0.1 mM P i ), which decreases the number of viable cells from 6 ؋ 10 8 to <10 CFU/ml between days 6 and 14 of incubation. Here we show that following two serial transfers into P i -limiting medium, evolved mutants survived prolonged incubation (Ϸ10 7 CFU/ml on day 14 of incubation). The evolved strains that overtook the populations were generally PhnE ؉ , whereas the ancestral K-12 strain carries an inactive phnE allele, which prevents the transport of phosphonates. The switching in phnE occurred with a high frequency as a result of the deletion of an 8-bp repeated sequence. In a mixed culture starved for P i that contained the K-12 ancestral strain in majority, evolved strains grew through PhnE-dependent scavenging of probably organic phosphate esters (not phosphonates or P i ) released by E. coli K-12 between days 1 and 3, before acetic acid excreted by E. coli K-12 reached toxic levels. The growth yield of phnE ؉ strains in mixed culture was dramatically enhanced by mutations that affect glucose metabolism, such as an rpoS mutation inactivating the alternative sigma factor RpoS. The longterm viability of evolved populations was generally higher when the ancestral strain carried an inactive rather than an active phnE allele, which indicates that cross-feeding of phosphorylated products as a result of the phnE polymorphism may be essential for the spread of mutants which eventually help populations to survive under P i starvation conditions.

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Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway

Cited by 65 publications

References 27 publications

Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Utilization of Glyphosate as Phosphate Source: Biochemistry and Genetics of Bacterial Carbon-Phosphorus Lyase

Antibodies to PhnD Inhibit Staphylococcal Biofilms

Activation of the Cryptic PhnE Permease Promotes Rapid Adaptive Evolution in a Population of Escherichia coli K-12 Starved for Phosphate

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