The IalA invasion gene of Bartonella bacilliformis encodes a (di)nucleoside polyphosphate hydrolase of the MutT motif family and has homologs in other invasive bacteria

Jared L. Cartwright, Phillipa Britton, Michael F. Minnick, Alexander G. McLennan

Research output: Contribution to journalArticlepeer-review

Abstract

The product of the ialA invasion gene of Bartonella bacilliformis has been expressed as a thioredoxin fusion protein. It is a (di)nucleoside polyphosphate hydrolase of the MutT motif protein family with strong sequence similarity to plant diadenosine tetraphosphate hydrolases. It hydrolyses nucleoside and dinucleoside polyphosphates with four or more phosphate groups, always producing an NTP as one product. Diadenosine tetraphosphate (Ap4A) is the preferred substrate with a K(m) of 10 μM and a k(cat) of 3.0 s-1. It is inhibited by Ca2+ and F- (K(i) = 30 μM). Hydrolysis of Ap4A in H218O yielded [18O]AMP as the only labelled product. In terms of sequence, reaction mechanism and properties, IalA is very similar to eukaryotic Ap4A hydrolases and unlike previously described bacterial Ap4A hydrolases. Homologs are present in the genomes of other invasive pathogens. They may function to reduce stress-induced dinucleotide levels during invasion and so enhance pathogen survival.

Original languageEnglish
Pages (from-to)474-479
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume256
Issue number3
DOIs
StatePublished - Mar 24 1999

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