Phosphorylation and dephosphorylation affect multiple bacterial properties

What is it about?

Burkholderia cenocepacia, a member of the B. cepacia complex (Bcc), is an opportunistic pathogen causing serious chronic in- fections in patients with cystic fibrosis. Tyrosine phosphorylation of bacterial proteins has emerged as an important posttranslational modification modulating the physiology and pathogenicity of Bcc bacteria. Here, we investigated the predicted bacterial tyrosine phosphorylating proteins (kinases) BCAM1331 and BceF and the low-molecular-weight protein tyrosine phosphatases BCAM0208, BceD, and BCAL2200 of B. cenocepacia K56-2.

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Why is it important?

We show that despite having similar biochemical activities, low- molecular-weight protein tyrosine phosphatases and tyrosine kinases have both overlapping and specific roles in the physiology of B. cenocepacia.