Plant natriuretic peptides induce proteins diagnostic for an adaptive response to stress

Handle URI:
http://hdl.handle.net/10754/336429
Title:
Plant natriuretic peptides induce proteins diagnostic for an adaptive response to stress
Authors:
Turek, Ilona ( 0000-0001-6457-7456 ) ; Marondedze, Claudius ( 0000-0002-2113-904X ) ; Wheeler, Janet I.; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Irving, Helen R.
Abstract:
In plants, structural and physiological evidence has suggested the presence of biologically active natriuretic peptides (PNPs). PNPs are secreted into the apoplast, are systemically mobile and elicit a range of responses signaling via cGMP. The PNP-dependent responses include tissue specific modifications of cation transport and changes in stomatal conductance and the photosynthetic rate. PNP also has a critical role in host defense responses. Surprisingly, PNP-homologs are produced by several plant pathogens during host colonization suppressing host defense responses. Here we show that a synthetic peptide representing the biologically active fragment of the Arabidopsis thaliana PNP (AtPNP-A) induces the production of reactive oxygen species in suspension-cultured A. thaliana (Col-0) cells. To identify proteins whose expression changes in an AtPNP-A dependent manner, we undertook a quantitative proteomic approach, employing tandem mass tag (TMT) labeling, to reveal temporal responses of suspension-cultured cells to 1 nM and 10 pM PNP at two different time-points post-treatment. Both concentrations yield a distinct differential proteome signature. Since only the higher (1 nM) concentration induces a ROS response, we conclude that the proteome response at the lower concentration reflects a ROS independent response. Furthermore, treatment with 1 nM PNP results in an over-representation of the gene ontology (GO) terms “oxidation-reduction process,” “translation” and “response to salt stress” and this is consistent with a role of AtPNP-A in the adaptation to environmental stress conditions.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Turek I, Marondedze C, Wheeler JI, Gehring C and Irving HR (2014) Plant natriuretic peptides induce proteins diagnostic for an adaptive response to stress. Front. Plant Sci. 5:661. doi: 10.3389/fpls.2014.00661
Publisher:
Frontiers Media SA
Journal:
Frontiers in Plant Science
Issue Date:
26-Nov-2014
DOI:
10.3389/fpls.2014.00661
PubMed ID:
25505478
PubMed Central ID:
PMC4244590
Type:
Article
ISSN:
1664-462X
Additional Links:
http://www.frontiersin.org/Plant_Proteomics/10.3389/fpls.2014.00661/abstract
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorTurek, Ilonaen
dc.contributor.authorMarondedze, Claudiusen
dc.contributor.authorWheeler, Janet I.en
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorIrving, Helen R.en
dc.date.accessioned2014-12-01T15:45:30Z-
dc.date.available2014-12-01T15:45:30Z-
dc.date.issued2014-11-26en
dc.identifier.citationTurek I, Marondedze C, Wheeler JI, Gehring C and Irving HR (2014) Plant natriuretic peptides induce proteins diagnostic for an adaptive response to stress. Front. Plant Sci. 5:661. doi: 10.3389/fpls.2014.00661en
dc.identifier.issn1664-462Xen
dc.identifier.pmid25505478en
dc.identifier.doi10.3389/fpls.2014.00661en
dc.identifier.urihttp://hdl.handle.net/10754/336429en
dc.description.abstractIn plants, structural and physiological evidence has suggested the presence of biologically active natriuretic peptides (PNPs). PNPs are secreted into the apoplast, are systemically mobile and elicit a range of responses signaling via cGMP. The PNP-dependent responses include tissue specific modifications of cation transport and changes in stomatal conductance and the photosynthetic rate. PNP also has a critical role in host defense responses. Surprisingly, PNP-homologs are produced by several plant pathogens during host colonization suppressing host defense responses. Here we show that a synthetic peptide representing the biologically active fragment of the Arabidopsis thaliana PNP (AtPNP-A) induces the production of reactive oxygen species in suspension-cultured A. thaliana (Col-0) cells. To identify proteins whose expression changes in an AtPNP-A dependent manner, we undertook a quantitative proteomic approach, employing tandem mass tag (TMT) labeling, to reveal temporal responses of suspension-cultured cells to 1 nM and 10 pM PNP at two different time-points post-treatment. Both concentrations yield a distinct differential proteome signature. Since only the higher (1 nM) concentration induces a ROS response, we conclude that the proteome response at the lower concentration reflects a ROS independent response. Furthermore, treatment with 1 nM PNP results in an over-representation of the gene ontology (GO) terms “oxidation-reduction process,” “translation” and “response to salt stress” and this is consistent with a role of AtPNP-A in the adaptation to environmental stress conditions.en
dc.language.isoenen
dc.publisherFrontiers Media SAen
dc.relation.urlhttp://www.frontiersin.org/Plant_Proteomics/10.3389/fpls.2014.00661/abstracten
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en
dc.subjectplant natriuretic peptideen
dc.subjectpeptide hormone signalingen
dc.subjectplant homeostasisen
dc.subjectmolecular mimicryen
dc.subjectsalt stressen
dc.subjectreactive oxygen speciesen
dc.titlePlant natriuretic peptides induce proteins diagnostic for an adaptive response to stressen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalFrontiers in Plant Scienceen
dc.identifier.pmcidPMC4244590en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Melbourne, VIC, Australiaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorMarondedze, Claudiusen
kaust.authorGehring, Christoph A.en
kaust.authorTurek, Lionsen
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