Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome
Basal phosphoinositide-dependent phospholipase C (PI-PLC) activity controls gene expression in Arabidopsis suspension cells and seedlings. PI-PLC catalyzes the production of phosphorylated inositol and diacylglycerol (DAG) from phosphoinositides. It is not known how PI-PLC regulates the transcriptom...
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2014-11-01
|
Series: | Frontiers in Plant Science |
Subjects: | |
Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00608/full |
_version_ | 1818423296313524224 |
---|---|
author | Eric eRuelland Eric eRuelland Eric eRuelland Igor ePokotylo Igor ePokotylo Catherine eCantrel Catherine eCantrel Nabila eDjafi Anne eRepellin Alain eZachowski Alain eZachowski Alain eZachowski |
author_facet | Eric eRuelland Eric eRuelland Eric eRuelland Igor ePokotylo Igor ePokotylo Catherine eCantrel Catherine eCantrel Nabila eDjafi Anne eRepellin Alain eZachowski Alain eZachowski Alain eZachowski |
author_sort | Eric eRuelland |
collection | DOAJ |
description | Basal phosphoinositide-dependent phospholipase C (PI-PLC) activity controls gene expression in Arabidopsis suspension cells and seedlings. PI-PLC catalyzes the production of phosphorylated inositol and diacylglycerol (DAG) from phosphoinositides. It is not known how PI-PLC regulates the transcriptome although the action of DAG-kinase (DGK) on DAG immediately downstream from PI-PLC is responsible for some of the regulation. We previously established a list of genes whose expression is affected in the presence of PI-PLC inhibitors. Here this list of genes was used as a signature in similarity searches of curated plant hormone response transcriptome data. The strongest correlations obtained with the inhibited PI-PLC signature were with salicylic acid (SA) treatments. We confirm here that in Arabidopsis suspension cells SA treatment leads to an increase in phosphoinositides, then demonstrate that SA leads to a significant 20% decrease in phosphatidic acid, indicative of a decrease in PI-PLC products. Previous sets of microarray data were re-assessed. The SA response of one set of genes was dependent on phosphoinositides. Alterations in the levels of a second set of genes, mostly SA-repressed genes, could be related to decreases in PI-PLC products that occur in response to SA action. Together, the two groups of genes comprise at least 40% of all SA-responsive genes. Overall these two groups of genes are distinct in the functional categories of the proteins they encode, their promoter cis-elements and their regulation by DGK or phospholipase D. SA-regulated genes dependent on phosphoinositides are typical SA response genes while those with an SA response that is possibly dependent on PI-PLC products are less SA-specific. We propose a model in which SA inhibits PI-PLC activity and alters levels of PI-PLC products and substrates, thereby regulating gene expression divergently. |
first_indexed | 2024-12-14T13:39:54Z |
format | Article |
id | doaj.art-266137da4dee4513b25bbfdc7178cb8c |
institution | Directory Open Access Journal |
issn | 1664-462X |
language | English |
last_indexed | 2024-12-14T13:39:54Z |
publishDate | 2014-11-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Plant Science |
spelling | doaj.art-266137da4dee4513b25bbfdc7178cb8c2022-12-21T22:59:28ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2014-11-01510.3389/fpls.2014.00608104890Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptomeEric eRuelland0Eric eRuelland1Eric eRuelland2Igor ePokotylo3Igor ePokotylo4Catherine eCantrel5Catherine eCantrel6Nabila eDjafi7Anne eRepellin8Alain eZachowski9Alain eZachowski10Alain eZachowski11Centre National de la Recherche ScientifiqueUniversité Paris-Est CréteilCentre National de la Recherche ScientifiqueUniversité Paris-Est CréteilNational academy of Sciences of UkraineCentre National de la Recherche ScientifiqueCentre National de la Recherche ScientifiqueCentre National de la Recherche ScientifiqueUniversité Paris-Est CréteilCentre National de la Recherche ScientifiqueUniversité Paris-Est CréteilCentre National de la Recherche ScientifiqueBasal phosphoinositide-dependent phospholipase C (PI-PLC) activity controls gene expression in Arabidopsis suspension cells and seedlings. PI-PLC catalyzes the production of phosphorylated inositol and diacylglycerol (DAG) from phosphoinositides. It is not known how PI-PLC regulates the transcriptome although the action of DAG-kinase (DGK) on DAG immediately downstream from PI-PLC is responsible for some of the regulation. We previously established a list of genes whose expression is affected in the presence of PI-PLC inhibitors. Here this list of genes was used as a signature in similarity searches of curated plant hormone response transcriptome data. The strongest correlations obtained with the inhibited PI-PLC signature were with salicylic acid (SA) treatments. We confirm here that in Arabidopsis suspension cells SA treatment leads to an increase in phosphoinositides, then demonstrate that SA leads to a significant 20% decrease in phosphatidic acid, indicative of a decrease in PI-PLC products. Previous sets of microarray data were re-assessed. The SA response of one set of genes was dependent on phosphoinositides. Alterations in the levels of a second set of genes, mostly SA-repressed genes, could be related to decreases in PI-PLC products that occur in response to SA action. Together, the two groups of genes comprise at least 40% of all SA-responsive genes. Overall these two groups of genes are distinct in the functional categories of the proteins they encode, their promoter cis-elements and their regulation by DGK or phospholipase D. SA-regulated genes dependent on phosphoinositides are typical SA response genes while those with an SA response that is possibly dependent on PI-PLC products are less SA-specific. We propose a model in which SA inhibits PI-PLC activity and alters levels of PI-PLC products and substrates, thereby regulating gene expression divergently.http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00608/fullArabidopsisDiacylglycerol KinaseSalicylic Acidlipid signalingphospholipase Ctrancriptomic |
spellingShingle | Eric eRuelland Eric eRuelland Eric eRuelland Igor ePokotylo Igor ePokotylo Catherine eCantrel Catherine eCantrel Nabila eDjafi Anne eRepellin Alain eZachowski Alain eZachowski Alain eZachowski Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome Frontiers in Plant Science Arabidopsis Diacylglycerol Kinase Salicylic Acid lipid signaling phospholipase C trancriptomic |
title | Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome |
title_full | Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome |
title_fullStr | Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome |
title_full_unstemmed | Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome |
title_short | Salicylic acid modulates levels of phosphoinositide dependent-phospholipase C substrates and products to remodel the Arabidopsis suspension cell transcriptome |
title_sort | salicylic acid modulates levels of phosphoinositide dependent phospholipase c substrates and products to remodel the arabidopsis suspension cell transcriptome |
topic | Arabidopsis Diacylglycerol Kinase Salicylic Acid lipid signaling phospholipase C trancriptomic |
url | http://journal.frontiersin.org/Journal/10.3389/fpls.2014.00608/full |
work_keys_str_mv | AT ericeruelland salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT ericeruelland salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT ericeruelland salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT igorepokotylo salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT igorepokotylo salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT catherineecantrel salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT catherineecantrel salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT nabilaedjafi salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT anneerepellin salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT alainezachowski salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT alainezachowski salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome AT alainezachowski salicylicacidmodulateslevelsofphosphoinositidedependentphospholipasecsubstratesandproductstoremodelthearabidopsissuspensioncelltranscriptome |