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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| Veröffentlicht in: | PloS one 2011-03, Vol.6 (3), p.e17767-e17767 |
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| creator | Meijer, H.J.G Hassen, H.H Govers, F |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0017767 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0017767</identifier><identifier>PMID: 21423760</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; activation ; Amino Acid Sequence ; Amino acids ; Biology ; Cell culture ; Cytoskeleton ; Enzymes ; Eukaryotes ; Evolution, Molecular ; Extracellular Space - enzymology ; Genes ; Genes - genetics ; Genomes ; Genomics ; Laboratories ; Lipids ; Metabolism ; Molecular Sequence Data ; Mutation ; Oomycetes ; Oryza - parasitology ; Pathogens ; Peptides ; Phosphatases ; Phosphatidic acid ; Phospholipase ; Phospholipase D ; Phospholipase D - chemistry ; Phospholipase D - classification ; Phospholipase D - genetics ; Phospholipase D - metabolism ; Phospholipases ; Phospholipids ; Phospholipids - metabolism ; Phylogeny ; Phytophthora ; Phytophthora infestans ; Phytophthora infestans - enzymology ; Phytophthora infestans - genetics ; Plant sciences ; Regulation ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal peptides ; Signal transduction ; Silybum marianum</subject><ispartof>PloS one, 2011-03, Vol.6 (3), p.e17767-e17767</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Meijer et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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.</description><subject>Acids</subject><subject>activation</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biology</subject><subject>Cell culture</subject><subject>Cytoskeleton</subject><subject>Enzymes</subject><subject>Eukaryotes</subject><subject>Evolution, Molecular</subject><subject>Extracellular Space - enzymology</subject><subject>Genes</subject><subject>Genes - genetics</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Laboratories</subject><subject>Lipids</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Oomycetes</subject><subject>Oryza - parasitology</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Phosphatases</subject><subject>Phosphatidic acid</subject><subject>Phospholipase</subject><subject>Phospholipase D</subject><subject>Phospholipase D - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>NARCIS:Publications</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meijer, H.J.G</au><au>Hassen, H.H</au><au>Govers, F</au><au>Badger, Jonathan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phytophthora infestans has a plethora of phospholipase D enzymes including a subclass that has extracellular activity</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-03-14</date><risdate>2011</risdate><volume>6</volume><issue>3</issue><spage>e17767</spage><epage>e17767</epage><pages>e17767-e17767</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21423760</pmid><doi>10.1371/journal.pone.0017767</doi><tpages>e17767</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acids activation Amino Acid Sequence Amino acids Biology Cell culture Cytoskeleton Enzymes Eukaryotes Evolution, Molecular Extracellular Space - enzymology Genes Genes - genetics Genomes Genomics Laboratories Lipids Metabolism Molecular Sequence Data Mutation Oomycetes Oryza - parasitology Pathogens Peptides Phosphatases Phosphatidic acid Phospholipase Phospholipase D Phospholipase D - chemistry Phospholipase D - classification Phospholipase D - genetics Phospholipase D - metabolism Phospholipases Phospholipids Phospholipids - metabolism Phylogeny Phytophthora Phytophthora infestans Phytophthora infestans - enzymology Phytophthora infestans - genetics Plant sciences Regulation Sequence Alignment Sequence Homology, Amino Acid Signal peptides Signal transduction Silybum marianum |
| title | Phytophthora infestans has a plethora of phospholipase D enzymes including a subclass that has extracellular activity |
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