Loss of chloroplast‐localized protein phosphatase 2Cs in Arabidopsis thaliana leads to enhancement of plant immunity and resistance to Xanthomonas campestris pv. campestris infection

Summary Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a sp...

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Published inMolecular plant pathology Vol. 19; no. 5; pp. 1184 - 1195
Main Authors Akimoto‐Tomiyama, Chiharu, Tanabe, Shigeru, Kajiwara, Hideyuki, Minami, Eiichi, Ochiai, Hirokazu
Format Journal Article
LanguageEnglish
Published England John Wiley & Sons, Inc 01.05.2018
John Wiley and Sons Inc
Subjects
Arabidopsis - enzymology
Arabidopsis - immunology
Arabidopsis - microbiology
Arabidopsis Proteins - metabolism
Arabidopsis thaliana
Bacterial Secretion Systems
Black rot
Blight
chloroplast
Chloroplasts
Chloroplasts - enzymology
Crosstalk
Disease Resistance
Eukaryotes
Gel electrophoresis
Gene Expression Regulation, Plant
Immune system
Immunity
Infections
Isoelectric focusing
Kinases
Mutants
Mutation - genetics
Nicotiana - metabolism
Original
Oryza
Phosphorylation
Photosynthesis
Plant Diseases - immunology
Plant Diseases - microbiology
Plant Immunity
Protein phosphatase
protein phosphatase 2C
Protein Phosphatase 2C - metabolism
Proteins
Serine
Signal transduction
Sodium
Sodium lauryl sulfate
Subgroups
Substrate Specificity
Substrates
Threonine
Transduction
type III secretion system, Xanthomonas campestris pv. campestris
Xanthomonas campestris
Xanthomonas campestris - growth & development
Xanthomonas campestris - pathogenicity
Arabidopsis thaliana
type III secretion system, Xanthomonas campestris pv. campestris
chloroplast
protein phosphatase 2C
plant immunity
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Abstract Summary Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight. In Arabidopsis thaliana, orthologous PP2C genes (AtPP2C62 and AtPP2C26) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris (Xcc, causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62‐ and atpp2c26‐deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis‐related protein, chaperonin‐60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two‐dimensional isoelectric focusing sodium dodecylsulfate‐polyacrylamide gel electrophoresis (2D‐IDF‐SDS‐PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
AbstractList Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine-specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight. In Arabidopsis thaliana, orthologous PP2C genes (AtPP2C62 and AtPP2C26) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris (Xcc, causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62- and atpp2c26-deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis-related protein, chaperonin-60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two-dimensional isoelectric focusing sodium dodecylsulfate-polyacrylamide gel electrophoresis (2D-IDF-SDS-PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight. In Arabidopsis thaliana, orthologous PP2C genes (AtPP2C62 and AtPP2C26) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris (Xcc, causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62‐ and atpp2c26‐deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis‐related protein, chaperonin‐60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two‐dimensional isoelectric focusing sodium dodecylsulfate‐polyacrylamide gel electrophoresis (2D‐IDF‐SDS‐PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
Summary Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae , the causal agent of bacterial blight. In Arabidopsis thaliana , orthologous PP2C genes ( AtPP2C62 and AtPP2C26 ) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris ( Xcc , causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62 ‐ and atpp2c26 ‐deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis‐related protein, chaperonin‐60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two‐dimensional isoelectric focusing sodium dodecylsulfate‐polyacrylamide gel electrophoresis (2D‐IDF‐SDS‐PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
Summary Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight. In Arabidopsis thaliana, orthologous PP2C genes (AtPP2C62 and AtPP2C26) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris (Xcc, causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62‐ and atpp2c26‐deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis‐related protein, chaperonin‐60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two‐dimensional isoelectric focusing sodium dodecylsulfate‐polyacrylamide gel electrophoresis (2D‐IDF‐SDS‐PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of the serine/threonine‐specific PP family, are greatly expanded in plants. Thus, PP2Cs are thought to play a specific role in signal transduction pathways. Some rice PP2Cs classified in subgroup K are responsive to infection by the compatible Xanthomonas oryzae pv. oryzae , the causal agent of bacterial blight. In Arabidopsis thaliana , orthologous PP2C genes ( AtPP2C62 and AtPP2C26 ) classified to subgroup K are also responsive to Xanthomonas campestris pv. campestris ( Xcc , causal agent of black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62 ‐ and atpp2c26 ‐deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development, as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, the photosynthesis‐related protein, chaperonin‐60, was indicated as the potential candidate for the dephosphorylated substrate catalysed by AtPP2C62 and AtPP2C26 using two‐dimensional isoelectric focusing sodium dodecylsulfate‐polyacrylamide gel electrophoresis (2D‐IDF‐SDS‐PAGE). Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of the plant immune system. These results imply the occurrence of crosstalk between photosynthesis and the plant defence system to control productivity under pathogen infection.
Author Ochiai, Hirokazu
Kajiwara, Hideyuki
Akimoto‐Tomiyama, Chiharu
Tanabe, Shigeru
Minami, Eiichi
AuthorAffiliation 2 Advanced Analysis Center National Agriculture and Food Research Organization Tsukuba Ibaraki 305‐8602, Japan
1 Institute of Agrobiological Sciences, National Agriculture and Food Research Organization Tsukuba Ibaraki 305‐8602, Japan
3 Present address: Sakata Seed Corporation Yokohama Japan
AuthorAffiliation_xml – name: 2 Advanced Analysis Center National Agriculture and Food Research Organization Tsukuba Ibaraki 305‐8602, Japan
– name: 3 Present address: Sakata Seed Corporation Yokohama Japan
– name: 1 Institute of Agrobiological Sciences, National Agriculture and Food Research Organization Tsukuba Ibaraki 305‐8602, Japan
Author_xml – sequence: 1
  givenname: Chiharu
  surname: Akimoto‐Tomiyama
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  givenname: Shigeru
  surname: Tanabe
  fullname: Tanabe, Shigeru
  organization: Institute of Agrobiological Sciences, National Agriculture and Food Research Organization
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  surname: Minami
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  organization: Institute of Agrobiological Sciences, National Agriculture and Food Research Organization
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  givenname: Hirokazu
  surname: Ochiai
  fullname: Ochiai, Hirokazu
  organization: Institute of Agrobiological Sciences, National Agriculture and Food Research Organization
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Keywords Arabidopsis thaliana
type III secretion system, Xanthomonas campestris pv. campestris
chloroplast
protein phosphatase 2C
plant immunity
Language English
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SSID ssj0017925
Score 2.3569543
Snippet Summary Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs,...
Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of...
SourceID pubmedcentral
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wiley
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 1184
SubjectTerms Arabidopsis - enzymology
Arabidopsis - immunology
Arabidopsis - microbiology
Arabidopsis Proteins - metabolism
Arabidopsis thaliana
Bacterial Secretion Systems
Black rot
Blight
chloroplast
Chloroplasts
Chloroplasts - enzymology
Crosstalk
Disease Resistance
Eukaryotes
Gel electrophoresis
Gene Expression Regulation, Plant
Immune system
Immunity
Infections
Isoelectric focusing
Kinases
Mutants
Mutation - genetics
Nicotiana - metabolism
Original
Oryza
Phosphorylation
Photosynthesis
Plant Diseases - immunology
Plant Diseases - microbiology
Plant Immunity
Protein phosphatase
protein phosphatase 2C
Protein Phosphatase 2C - metabolism
Proteins
Serine
Signal transduction
Sodium
Sodium lauryl sulfate
Subgroups
Substrate Specificity
Substrates
Threonine
Transduction
type III secretion system, Xanthomonas campestris pv. campestris
Xanthomonas campestris
Xanthomonas campestris - growth & development
Xanthomonas campestris - pathogenicity
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Title Loss of chloroplast‐localized protein phosphatase 2Cs in Arabidopsis thaliana leads to enhancement of plant immunity and resistance to Xanthomonas campestris pv. campestris infection
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fmpp.12596
https://www.ncbi.nlm.nih.gov/pubmed/28815858
https://www.proquest.com/docview/2023521719
https://pubmed.ncbi.nlm.nih.gov/PMC6637992
Volume 19
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