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PMID:25307893
| Citation |
'Dutta, S, Bhawsinghka, N and Das Gupta, SK (2014) Gp66, a calcineurin family phosphatase encoded by mycobacteriophage D29, is a 2', 3' cyclic nucleotide phosphodiesterase that negatively regulates phage growth. FEMS Microbiol. Lett. ' |
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| Abstract |
Mycobacteriophage D29 encodes a protein Gp66 which has been predicted to be a calcineurin family phosphoesterase. Phylogenetically Gp66 and related proteins mostly derived from mycobacteriophages form a distinct clade within this family. Interestingly, the presence of gene 66 orthologs can be traced to bacteria of diverse phylogenetic lineages such as Aquifex aeolicus, a deep branching eubacteria and Methanococcus jannaschii, an archaebacteria. The promiscuous nature of gene 66 suggests that it may have been transferred across genus barriers by horizontal gene transfer mechanisms. The biological function of members of this novel clade comprising mostly the mycobacteriophage phosphoesterases have not been elucidated so far. In this investigation, it has been demonstrated for the first time that Gp66, a member of this novel family, is a 2', 3' cyclic phosphodiesterase. The gene is expressed during phage infection and the net result is negative regulation of bacteriophage as well as bacterial growth. |
| Links |
PubMed Online version:10.1111/1574-6968.12625 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004112: cyclic-nucleotide phosphodiesterase activity |
ECO:0000314: |
F |
Figure 2 shows phosphoesterase activity of the gene product. Figure 3 compares activity to mutated genes and shows that phosphoesterase activity goes down for mutated genes. |
complete | ||||
| GO:0008081: phosphoric diester hydrolase activity |
ECO:0000314: |
F |
The gene Gp66 in mycobacteriophage D29 acts as a protein phosphatase. In the time span of 1 hour, protein dephosphorylation was observed when D29Gp66 was present (Fig 2B). Phosphoesterase assay using substrates pNPP, bis-pNPP and TmPP show that D29Gp66 can use both phosophomonoester and diester as substrates, with the catalytic activity for bis-NPP (diester) being ten times higher than pNPP (monoester) (Fig 2C). D29Gp66 appears to function mainly as a phosphodiesterase (Fig 2C). Gp66 has very high 2', 3' cyclic phosphodiesterase activity and no 3', 5' activity (Fig 2D). |
complete | ||||
Notes
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