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Degradation of polyphosphates by polyphosphate kinases from Ruegeria pomeroyi

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Abstract

Polyphosphate kinases 2 (PPK2) are key enzymes for polyphosphate utilisation in bacteria. The genome of Ruegeria pomeroyi, a marine α-proteobacterium, includes three Pseudomonas aeruginosa PPK2 homologs. We expressed these homologs in Escherichia coli as soluble proteins, purified the protein products and compared their metal, pH and nucleotide preferences. The optimal pH was 8.0 for SPO1727 and 9.0 for SPO1256. The SPO0224 gene product had two pH optima at eight and ten. The SPO0224 protein showed little dependence on metal presence, while SPO1256 required Mg2+. SPO1727 required Mg2+ but accepted other ions as well.

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Acknowledgments

This work was supported by the VEGA project No.: 2/0136/13. This contribution is the result of the project implementation: Centre of Excellence for White-Green Biotechnology, ITMS 26220120054, supported by the Research and Development Operational Programme funded by the ERDF.

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Authors and Affiliations

  1. Institute of Chemistry, Centre for Glycomics, Slovak Academy of Sciences, Dúbravská Cesta 9, 845 38, Bratislava, Slovakia

    Lucia Achbergerová & Jozef Nahálka

  2. Institute of Chemistry, Centre of Excellence for White-Green Biotechnology, Slovak Academy of Sciences, Trieda A. Hlinku 2, 949 76, Nitra, Slovakia

    Lucia Achbergerová & Jozef Nahálka

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  1. Lucia Achbergerová
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  2. Jozef Nahálka
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Correspondence to Jozef Nahálka.

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Achbergerová, L., Nahálka, J. Degradation of polyphosphates by polyphosphate kinases from Ruegeria pomeroyi . Biotechnol Lett 36, 2029–2035 (2014). https://doi.org/10.1007/s10529-014-1566-6

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  • DOI: https://doi.org/10.1007/s10529-014-1566-6

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