hemXis required for production of 2-ketogluconate, the predominant organic anion required for inorganic phosphate solubilization byBurkholderiasp. Ha185

    loading  Checking for direct PDF access through Ovid

Abstract

The bacteriumBurkholderiasp. Ha185 readily solubilizes inorganic phosphate by releasing the low molecular weight organic anion, 2-ketogluconate. Using random transposon mutagenesis andin silicoanalysis, a mutation that caused almost complete abolition of phosphate solubilization was located withinhemX, which is part of thehemoperon.Burkholderiasp. Ha185 HemX is a multidomain protein, predicted to encode a bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase, which has not previously been implicated in phosphate solubilization. Complementation ofhemXrestored the ability of the mutant to solubilize phosphate in both plate and liquid cultures. Based on a combination of organic-anion profiling, quantitative polymerase chain reaction andin silicoanalyses,hemXwas confirmed to be solely responsible for hydroxyapatite solubilization inBurkholderiasp. Ha185. It is proposed that the biosynthesis of a yet to be determined redox cofactor by HemX is the main pathway for generating 2-ketogluconate via a haem-dependent gluconate 2-dehydrogenase inBurkholderiasp. Ha185.

Related Topics

    loading  Loading Related Articles