An Unexpected Role for the Periplasmic Phosphatase PhoN in the Salvage of B6 Vitamers in Salmonella enterica.

Applied and Environmental Microbiology
Huong N Vu, Diana M Downs

Abstract

Pyridoxal 5'-phosphate (PLP) is the biologically active form of vitamin B6, essential for cellular function in all domains of life. In many organisms, such as Salmonella enterica serovar Typhimurium and Escherichia coli, this cofactor can be synthesized de novo or salvaged from B6 vitamers in the environment. Unexpectedly, S. enterica strains blocked in PLP biosynthesis were able to use exogenous PLP and pyridoxine 5'-phosphate (PNP) as the source of this required cofactor, while E. coli strains of the same genotype could not. Transposon mutagenesis found that phoN was essential for the salvage of PLP and PNP under the conditions tested. phoN encodes a class A nonspecific acid phosphatase (EC 3.1.3.2) that is transcriptionally regulated by the PhoPQ two-component system. The periplasmic location of PhoN was essential for PLP and PNP salvage, and in vitro assays confirmed PhoN has phosphatase activity with PLP and PNP as substrates. The data suggest that PhoN dephosphorylates B6 vitamers, after which they enter the cytoplasm and are phosphorylated by kinases of the canonical PLP salvage pathway. The connection of phoN with PhoPQ and the broad specificity of the gene product suggest S. enterica is exploiting a moonlighting activi...Continue Reading

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Citations

Sep 10, 2021·Molecular Microbiology·Huong N Vu, Diana M Downs

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