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GLYCINE‐RICH RNA‐BINDING PROTEIN1 interacts with RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 and suppresses cell death and defense responses in pepper (Capsicum annuum

Plants use a variety of innate immune regulators to trigger cell death and defense responses against pathogen attack. We identified pepper (Capsicum annuum) GLYCINE‐RICH RNA‐BINDING PROTEIN1 (CaGRP1) as a RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 (CaPIK1)‐interacting partner, based on bimolecular fl... Full description

Journal Title: New Phytologist January 2015, Vol.205(2), pp.786-800
Main Author: Kim, Dae Sung
Other Authors: Kim, Nak Hyun , Hwang, Byung Kook
Format: Electronic Article Electronic Article
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ID: ISSN: 0028-646X ; E-ISSN: 1469-8137 ; DOI: 10.1111/nph.13105
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title: GLYCINE‐RICH RNA‐BINDING PROTEIN1 interacts with RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 and suppresses cell death and defense responses in pepper (Capsicum annuum
format: Article
creator:
  • Kim, Dae Sung
  • Kim, Nak Hyun
  • Hwang, Byung Kook
subjects:
  • Cell Death
  • Dna And Rna Binding
  • Glycine‐Rich Rna ‐Binding Protein
  • Pepper C Apsicum Annuum
  • Plant Defense
  • Receptor‐Like Cytoplasmic Protein Kinase
  • X Anthomonas Campestris Pv Vesicatoria Xcv
ispartof: New Phytologist, January 2015, Vol.205(2), pp.786-800
description: Plants use a variety of innate immune regulators to trigger cell death and defense responses against pathogen attack. We identified pepper (Capsicum annuum) GLYCINE‐RICH RNA‐BINDING PROTEIN1 (CaGRP1) as a RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 (CaPIK1)‐interacting partner, based on bimolecular fluorescence complementation and coimmunoprecipitation analyses as well as gene silencing and transient expression analysis. CaGRP1 contains an N‐terminal RNA recognition motif and a glycine‐rich region at the C‐terminus. The CaGRP1 protein had DNA‐ and RNA‐binding activity in vitro. CaGRP1 interacted with CaPIK1 in planta. CaGRP1 and CaGRP1–CaPIK1 complexes were localized to the nucleus in plant cells. CaPIK1 phosphorylated CaGRP1 in vitro and in planta. Transient coexpression of CaGRP1 with CaPIK1 suppressed the CaPIK1‐triggered cell death response, accompanied by a reduced CaPIK1‐triggered reactive oxygen species (ROS) burst. The RNA recognition motif region of CaGRP1 was responsible for the nuclear localization of CaGRP1 as well as the suppression of the CaPIK1‐triggered cell death response. CaGRP1 silencing in pepper conferred enhanced resistance to Xanthomonas campestris pv vesicatoria (Xcv) infection; however, CaPIK1‐silenced plants were more susceptible to Xcv. CaGRP1 interacts with CaPIK1 and negatively regulates CaPIK1‐triggered cell death and defense responses by suppressing ROS accumulation.
language:
source:
identifier: ISSN: 0028-646X ; E-ISSN: 1469-8137 ; DOI: 10.1111/nph.13105
fulltext: fulltext
issn:
  • 0028-646X
  • 0028646X
  • 1469-8137
  • 14698137
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titleGLYCINE‐RICH RNA‐BINDING PROTEIN1 interacts with RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 and suppresses cell death and defense responses in pepper (Capsicum annuum
creatorKim, Dae Sung ; Kim, Nak Hyun ; Hwang, Byung Kook
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subjectCell Death ; Dna And Rna Binding ; Glycine‐Rich Rna ‐Binding Protein ; Pepper C Apsicum Annuum ; Plant Defense ; Receptor‐Like Cytoplasmic Protein Kinase ; X Anthomonas Campestris Pv Vesicatoria Xcv
descriptionPlants use a variety of innate immune regulators to trigger cell death and defense responses against pathogen attack. We identified pepper (Capsicum annuum) GLYCINE‐RICH RNA‐BINDING PROTEIN1 (CaGRP1) as a RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 (CaPIK1)‐interacting partner, based on bimolecular fluorescence complementation and coimmunoprecipitation analyses as well as gene silencing and transient expression analysis. CaGRP1 contains an N‐terminal RNA recognition motif and a glycine‐rich region at the C‐terminus. The CaGRP1 protein had DNA‐ and RNA‐binding activity in vitro. CaGRP1 interacted with CaPIK1 in planta. CaGRP1 and CaGRP1–CaPIK1 complexes were localized to the nucleus in plant cells. CaPIK1 phosphorylated CaGRP1 in vitro and in planta. Transient coexpression of CaGRP1 with CaPIK1 suppressed the CaPIK1‐triggered cell death response, accompanied by a reduced CaPIK1‐triggered reactive oxygen species (ROS) burst. The RNA recognition motif region of CaGRP1 was responsible for the nuclear localization of CaGRP1 as well as the suppression of the CaPIK1‐triggered cell death response. CaGRP1 silencing in pepper conferred enhanced resistance to Xanthomonas campestris pv vesicatoria (Xcv) infection; however, CaPIK1‐silenced plants were more susceptible to Xcv. CaGRP1 interacts with CaPIK1 and negatively regulates CaPIK1‐triggered cell death and defense responses by suppressing ROS accumulation.
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titleGLYCINE‐RICH RNA‐BINDING PROTEIN1 interacts with RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 and suppresses cell death and defense responses in pepper (Capsicum annuum
descriptionPlants use a variety of innate immune regulators to trigger cell death and defense responses against pathogen attack. We identified pepper (Capsicum annuum) GLYCINE‐RICH RNA‐BINDING PROTEIN1 (CaGRP1) as a RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 (CaPIK1)‐interacting partner, based on bimolecular fluorescence complementation and coimmunoprecipitation analyses as well as gene silencing and transient expression analysis. CaGRP1 contains an N‐terminal RNA recognition motif and a glycine‐rich region at the C‐terminus. The CaGRP1 protein had DNA‐ and RNA‐binding activity in vitro. CaGRP1 interacted with CaPIK1 in planta. CaGRP1 and CaGRP1–CaPIK1 complexes were localized to the nucleus in plant cells. CaPIK1 phosphorylated CaGRP1 in vitro and in planta. Transient coexpression of CaGRP1 with CaPIK1 suppressed the CaPIK1‐triggered cell death response, accompanied by a reduced CaPIK1‐triggered reactive oxygen species (ROS) burst. The RNA recognition motif region of CaGRP1 was responsible for the nuclear localization of CaGRP1 as well as the suppression of the CaPIK1‐triggered cell death response. CaGRP1 silencing in pepper conferred enhanced resistance to Xanthomonas campestris pv vesicatoria (Xcv) infection; however, CaPIK1‐silenced plants were more susceptible to Xcv. CaGRP1 interacts with CaPIK1 and negatively regulates CaPIK1‐triggered cell death and defense responses by suppressing ROS accumulation.
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titleGLYCINE‐RICH RNA‐BINDING PROTEIN1 interacts with RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 and suppresses cell death and defense responses in pepper (Capsicum annuum
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abstractPlants use a variety of innate immune regulators to trigger cell death and defense responses against pathogen attack. We identified pepper (Capsicum annuum) GLYCINE‐RICH RNA‐BINDING PROTEIN1 (CaGRP1) as a RECEPTOR‐LIKE CYTOPLASMIC PROTEIN KINASE1 (CaPIK1)‐interacting partner, based on bimolecular fluorescence complementation and coimmunoprecipitation analyses as well as gene silencing and transient expression analysis. CaGRP1 contains an N‐terminal RNA recognition motif and a glycine‐rich region at the C‐terminus. The CaGRP1 protein had DNA‐ and RNA‐binding activity in vitro. CaGRP1 interacted with CaPIK1 in planta. CaGRP1 and CaGRP1–CaPIK1 complexes were localized to the nucleus in plant cells. CaPIK1 phosphorylated CaGRP1 in vitro and in planta. Transient coexpression of CaGRP1 with CaPIK1 suppressed the CaPIK1‐triggered cell death response, accompanied by a reduced CaPIK1‐triggered reactive oxygen species (ROS) burst. The RNA recognition motif region of CaGRP1 was responsible for the nuclear localization of CaGRP1 as well as the suppression of the CaPIK1‐triggered cell death response. CaGRP1 silencing in pepper conferred enhanced resistance to Xanthomonas campestris pv vesicatoria (Xcv) infection; however, CaPIK1‐silenced plants were more susceptible to Xcv. CaGRP1 interacts with CaPIK1 and negatively regulates CaPIK1‐triggered cell death and defense responses by suppressing ROS accumulation.
doi10.1111/nph.13105
pages786-800
date2015-01