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PMID:26158264
Citation |
Mamberti, S, Prati, P, Cremaschi, P, Seppi, C, Morelli, CF, Galizzi, A, Fabbi, M and Calvio, C (2015) γ-PGA Hydrolases of Phage Origin in Bacillus subtilis and Other Microbial Genomes. PLoS ONE 10:e0130810 |
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Abstract |
Poly-γ-glutamate (γ-PGA) is an industrially interesting polymer secreted mainly by members of the class Bacilli which forms a shield able to protect bacteria from phagocytosis and phages. Few enzymes are known to degrade γ-PGA; among them is a phage-encoded γ-PGA hydrolase, PghP. The supposed role of PghP in phages is to ensure access to the surface of bacterial cells by dismantling the γ-PGA barrier. We identified four unannotated B. subtilis genes through similarity of their encoded products to PghP; in fact these genes reside in prophage elements of B. subtilis genome. The recombinant products of two of them demonstrate efficient polymer degradation, confirming that sequence similarity reflects functional homology. Genes encoding similar γ-PGA hydrolases were identified in phages specific for the order Bacillales and in numerous microbial genomes, not only belonging to that order. The distribution of the γ-PGA biosynthesis operon was also investigated with a bioinformatics approach; it was found that the list of organisms endowed with γ-PGA biosynthetic functions is larger than expected and includes several pathogenic species. Moreover in non-Bacillales bacteria the predicted γ-PGA hydrolase genes are preferentially found in species that do not have the genetic asset for polymer production. Our findings suggest that γ-PGA hydrolase genes might have spread across microbial genomes via horizontal exchanges rather than via phage infection. We hypothesize that, in natural habitats rich in γ-PGA supplied by producer organisms, the availability of hydrolases that release glutamate oligomers from γ-PGA might be a beneficial trait under positive selection. |
Links |
PubMed PMC4497714 Online version:10.1371/journal.pone.0130810 |
Keywords |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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GO:0016787: hydrolase activity |
ECO:0000314: |
F |
Enzyme assay viewed by gel separation shows that YndL reduces the molecular weight of y-PGA over time (Fig 3A), providing evidence that YndL is a y-PGA hydrolase. |
complete | ||||
GO:0016787: hydrolase activity |
ECO:0000314: |
F |
Enzyme assay viewed by gel separation shows that YoqZ reduces the molecular weight of y-PGA over time (Fig 3A), providing evidence that YoqZ is a y-PGA hydrolase. |
complete | ||||
Notes
See also
References
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