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Polygalacturonases (EC 3.2.1.15) catalyze the random hydrolysis of 1, 4-alpha-D-galactosiduronic linkages in pectate and other galacturonans.  Xylella fastidiosa  possesses a single polygalacturonase gene,  pglA  (PD1485), and  X .  fastidiosa  mutants deficient in the production of polygalacturonase are non-pathogenic and show a compromised ability to systemically infect grapevines. These results suggested that grapevines expressing sufficient amounts of an inhibitor of  X .  fastidiosa  polygalacturonase might be protected from disease. Previous work in our laboratory and others have tried without success to produce soluble active  X .  fastidiosa  polygalacturonase for use in inhibition assays. In this study, we created two enzymatically active  X .  fastidiosa / A .  vitis  polygalacturonase chimeras, AX1A and AX2A to explore the functionality of  X .  fastidiosa  polygalacturonase  in vitro . The AX1A chimera was constructed to specifically test if recombinant chimeric protein, produced in  Escherichia coli , is soluble and if the  X .  fastidiosa  polygalacturonase catalytic amino acids are able to hydrolyze polygalacturonic acid. The AX2A chimera was constructed to evaluate the ability of a unique QMK motif of  X .  fastidiosa  polygalacturonase, most polygalacturonases have a R(I/L)K motif, to bind to and allow the hydrolysis of polygalacturonic acid. Furthermore, the AX2A chimera was also used to explore what effect modification of the QMK motif of  X .  fastidiosa  polygalacturonase to a conserved RIK motif has on enzymatic activity. These experiments showed that both the AX1A and AX2A polygalacturonase chimeras were soluble and able to hydrolyze the polygalacturonic acid substrate. Additionally, the modification of the QMK motif to the conserved RIK motif eliminated hydrolytic activity, suggesting that the QMK motif is important for the activity of  X .  fastidiosa  polygalacturonase. This result suggests  X .  fastidiosa  polygalacturonase may preferentially hydrolyze a different pectic substrate or, alternatively, it has a different mechanism of substrate binding than other polygalacturonases characterized to date.

plos one

Insights into the Activity and Substrate Binding of Xylella fastidiosa Polygalacturonase by Modification of a Unique QMK Amino Acid Motif Using Protein Chimeras