Pseudomonas syringae dual-function protein Lon switches between virulence and metabolism by acting as both DNA-binding transcriptional regulator and protease in different environments.

: Lon, a member of the AAA+ protease family, plays vital roles in type III secretion systems (T3SS), agglutination and colony shape in the model plant pathogen Pseudomonas syringae. Lon also functions as a transcriptional regulator in other bacterial species such as Escherichia coli and Brevibacillus thermoruber. To reveal the molecular mechanisms of Lon as a dual-function protein in P. syringae, we studied Lon-regulated genes by using RNA sequencing (RNA-seq), chromatin immunoprecipitation sequencing (ChIP-seq), and liquid chromatography-tandem mass spectrometry (LC-MS/MS). As a transcriptional regulator, Lon directly regulated a group of genes (PSPPH_4788, gacA, fur, gntR, clpS, lon and glyA), and consequently regulated their functions, such as 1-dodecanol oxidation activity, motility, pyoverdine production, glucokinase activity, N-end rule pathway, lon expression and serine hydroxymethyltransferase (SHMT) activity. Mass spectrometry results revealed that the expression levels of 5 T3SS proteins (such as HrcV, HrpW1) were higher in the ∆lon strain than the wild-type strain in KB. In MM, 12 metabolic proteins (such as AcdS and NuoI) showed lower levels in the ∆lon strain than the wild-type strain. Taken together, these data demonstrate that the dual-function protein Lon sophisticatedly regulates virulence and metabolism in P. syringae.