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The acylase PvdQ has a conserved function among fluorescent Pseudomonas spp

Gudrun Koch1, Pol Nadal Jimenez, Remco Muntendam

  • 1Department of Pharmaceutical Biology, 9713AV Groningen, the Netherlands. School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, Nottingham NG7 2RD, UK.

Environmental Microbiology Reports
|June 15, 2013
PubMed

Insights

The enzyme PvdQ is crucial for pyoverdine production in Pseudomonas species. Its role in degrading quorum-sensing signals appears unique to Pseudomonas aeruginosa, unlike its conserved function in pyoverdine biosynthesis across related bacteria.

Area of Science:

  • Microbiology
  • Biochemistry
  • Bacterial Genetics

Background:

  • Pyoverdine is a key siderophore for iron uptake in fluorescent Pseudomonas species.
  • The enzyme PvdQ is essential for pyoverdine maturation and can degrade N-acyl homoserine lactones (AHLs), which are bacterial quorum-sensing molecules.
  • The genomic organization of the pvdQ gene varies among Pseudomonas species, being part of the pyoverdine cluster in some but not others.

Purpose of the Study:

  • To compare the enzymatic activities of PvdQ orthologues from different Pseudomonas species.
  • To investigate the conserved and unique functions of PvdQ in pyoverdine biosynthesis and quorum-sensing signal degradation.
  • To determine the regulatory mechanisms controlling pvdQ gene expression.

Main Methods:

  • Comparative analysis of PvdQ orthologues from Pseudomonas fluorescens PfO-1, P. putida KT2440, and P. aeruginosa PA14.
  • Enzyme activity assays to assess substrate specificity for AHLs.
  • Gene expression studies to examine regulation by iron availability.

Main Results:

  • PvdQ orthologues from P. fluorescens, P. putida, and P. aeruginosa exhibit conserved functions in pyoverdine production.
  • All tested PvdQ orthologues demonstrate conserved substrate specificity for AHLs.
  • Expression of pvdQ orthologues is consistently regulated by iron availability across different species.
  • The ability of PvdQ to control quorum-sensing signals appears to be a unique trait of P. aeruginosa.

Conclusions:

  • The role of PvdQ in pyoverdine biosynthesis is conserved across various Pseudomonas species.
  • PvdQ possesses conserved enzymatic activity towards AHLs, suggesting a broader functional role beyond pyoverdine maturation.
  • Iron availability is a conserved regulatory factor for pvdQ gene expression.
  • The regulation of quorum-sensing by PvdQ is a specialized function likely unique to P. aeruginosa.

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