Phytophthora infestans has a plethora of phospholipase D enzymes including a subclass that has extracellular activity.

Harold J G Meijer,Francine Govers,Hussen Harrun Hassen

doi:10.1371/journal.pone.0017767

Harold J G Meijer, Francine Govers + Show 1 more

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https://doi.org/10.1371/journal.pone.0017767

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Journal: PloS one	Publication Date: Mar 14, 2011
Citations: 34	License type: CC BY 4.0

Affiliation: Centre for BioSystems Genomics

Abstract

In eukaryotes phospholipase D (PLD) is involved in many cellular processes. Currently little is known about PLDs in oomycetes. Here we report that the oomycete plant pathogen Phytophthora infestans has a large repertoire of PLDs divided over six subfamilies: PXPH-PLD, PXTM-PLD, TM-PLD, PLD-likes, and type A and B sPLD-likes. Since the latter have signal peptides we developed a method using metabolically labelled phospholipids to monitor if P. infestans secretes PLD. In extracellular medium of ten P. infestans strains PLD activity was detected as demonstrated by the production of phosphatidic acid and the PLD specific marker phosphatidylalcohol.

Highlights

In eukaryotes, phospholipid-based signalling and metabolism play important roles in numerous cellular processes
The genome sequence of P. infestans harbours eighteen genes encoding a Phospholipase D (PLD), all of which can be classified in the subfamilies identified previously in P. sojae and P. ramorum (Table 1)
Eighteen PLD genes were identified in the genome of P. infestans and this correlates with findings in P. sojae and P. ramorum [4]

Summary

Introduction

Phospholipid-based signalling and metabolism play important roles in numerous cellular processes. Phospholipase D (PLD) catalyzes the hydrolysis of structural phospholipids at their terminal phosphoesteric bond, leading to the production of a hydrophilic constituent and phosphatidic acid (PA). The latter has emerged as a significant lipid mediator in many cellular processes. All eukaryotes have PXPH-PLDs that are composed of the N-terminally located phosphoinositide binding domains Pleckstrin homology (PH) and PHOX homology (PX) These precede the catalytic site and regulatory motifs. Unique to plants are the C2PLDs that contain the N-terminally located calcium/lipid binding domain C2 These two PLD subfamilies have a catalytic site with two highly conserved motifs each consisting of HxKxxxxD (hereafter HKD1 and HKD2). A novel rice (Oryza sativa) PLD was described that contains the two HKD motifs as well as a N-terminal signal peptide (SP) [3]

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