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Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity

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, an...

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Detalles Bibliográficos
Autores principales: Meijer, Harold J. G., Hassen, Hussen Harrun, Govers, Francine
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3056787/
https://www.ncbi.nlm.nih.gov/pubmed/21423760
http://dx.doi.org/10.1371/journal.pone.0017767
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author Meijer, Harold J. G.
Hassen, Hussen Harrun
Govers, Francine
author_facet Meijer, Harold J. G.
Hassen, Hussen Harrun
Govers, Francine
author_sort Meijer, Harold J. G.
collection PubMed
description 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.
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spelling pubmed-30567872011-03-18 Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity Meijer, Harold J. G. Hassen, Hussen Harrun Govers, Francine PLoS One Research Article 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. Public Library of Science 2011-03-14 /pmc/articles/PMC3056787/ /pubmed/21423760 http://dx.doi.org/10.1371/journal.pone.0017767 Text en Meijer et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Meijer, Harold J. G.
Hassen, Hussen Harrun
Govers, Francine
Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title_full Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title_fullStr Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title_full_unstemmed Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title_short Phytophthora infestans Has a Plethora of Phospholipase D Enzymes Including a Subclass That Has Extracellular Activity
title_sort phytophthora infestans has a plethora of phospholipase d enzymes including a subclass that has extracellular activity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3056787/
https://www.ncbi.nlm.nih.gov/pubmed/21423760
http://dx.doi.org/10.1371/journal.pone.0017767
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