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The pepper patatin-like phospholipase CaPLP1 functions in plant cell death and defense signaling

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dc.contributor.authorKim, Dae Sung-
dc.contributor.authorJeun, Yongchull-
dc.contributor.authorHwang, Byung Kook-
dc.date.accessioned2021-09-05T11:54:26Z-
dc.date.available2021-09-05T11:54:26Z-
dc.date.created2021-06-15-
dc.date.issued2014-02-
dc.identifier.issn0167-4412-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/99451-
dc.description.abstractPhospholipases hydrolyze phospholipids into fatty acids and other lipophilic substances. Phospholipid signaling is crucial for diverse cellular processes in plants. However, the precise role of phospholipases in plant cell death and defense signaling is not fully understood. Here, we identified a pepper (Capsicum annuum) patatin-like phospholipase (CaPLP1) gene that is transcriptionally induced in pepper leaves by avirulent Xanthomonas campestris pv. vesicatoria (Xcv) infection. CaPLP1 containing an N-terminal signal peptide localized to the cytoplasm and plasma membrane, leading to the secretion into the apoplastic regions. Silencing of CaPLP1 in pepper conferred enhanced susceptibility to Xcv infection. Defense responses to Xcv, including the generation of reactive oxygen species (ROS), hypersensitive cell death and the expression of the salicylic acid (SA)-dependent marker gene CaPR1, were compromised in the CaPLP1-silenced pepper plants. Transient expression of CaPLP1 in pepper leaves induced the accumulation of fluorescent phenolics, expression of the defense marker genes CaPR1 and CaSAR82A, and generation of ROS, ultimately leading to the hypersensitive cell death response. Overexpression (OX) of CaPLP1 in Arabidopsis also conferred enhanced resistance to Pseudomonas syringae pv. tomato (Pst) and Hyaloperonospora arabidopsidis infection. CaPLP1-OX leaves showed reduced Pst growth, enhanced ROS burst and electrolyte leakage, induction of the defense response genes AtPR1, AtRbohD and AtGST, as well as constitutive activation of both the SA-dependent gene AtPR1 and the JA-dependent gene AtPDF1.2. Together, these results suggest that CaPLP1 is involved in plant defense and cell death signaling in response to microbial pathogens.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherSPRINGER-
dc.subjectLIPID ACYL HYDROLASE-
dc.subjectMICROBIAL PATHOGENS-
dc.subjectCAPSICUM-ANNUUM-
dc.subjectSALICYLIC-ACID-
dc.subjectENVIRONMENTAL-STRESSES-
dc.subjectARABIDOPSIS-THALIANA-
dc.subjectDISEASE RESISTANCE-
dc.subjectABIOTIC ELICITORS-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectTOBACCO-LEAVES-
dc.titleThe pepper patatin-like phospholipase CaPLP1 functions in plant cell death and defense signaling-
dc.typeArticle-
dc.contributor.affiliatedAuthorHwang, Byung Kook-
dc.identifier.doi10.1007/s11103-013-0137-x-
dc.identifier.scopusid2-s2.0-84890884362-
dc.identifier.wosid000330980600007-
dc.identifier.bibliographicCitationPLANT MOLECULAR BIOLOGY, v.84, no.3, pp.329 - 344-
dc.relation.isPartOfPLANT MOLECULAR BIOLOGY-
dc.citation.titlePLANT MOLECULAR BIOLOGY-
dc.citation.volume84-
dc.citation.number3-
dc.citation.startPage329-
dc.citation.endPage344-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaPlant Sciences-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryPlant Sciences-
dc.subject.keywordPlusLIPID ACYL HYDROLASE-
dc.subject.keywordPlusMICROBIAL PATHOGENS-
dc.subject.keywordPlusCAPSICUM-ANNUUM-
dc.subject.keywordPlusSALICYLIC-ACID-
dc.subject.keywordPlusENVIRONMENTAL-STRESSES-
dc.subject.keywordPlusARABIDOPSIS-THALIANA-
dc.subject.keywordPlusDISEASE RESISTANCE-
dc.subject.keywordPlusABIOTIC ELICITORS-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusTOBACCO-LEAVES-
dc.subject.keywordAuthorCapsicum annuum-
dc.subject.keywordAuthorXanthomonas campestris pv. vesicatoria-
dc.subject.keywordAuthorPatatin-like phospholipase-
dc.subject.keywordAuthorCell death-
dc.subject.keywordAuthorPlant defense-
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