Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice

Yusuke Kouzai, Hanae Kaku, Naoto Shibuya, Eiichi Minami, Yoko Nishizawa

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

We previously reported that rice plants expressing the chimeric receptor consisting of rice chitin oligosaccharides binding protein (CEBiP) and the intracellular protein kinase region of Xa21, which confers resistance to rice bacterial blight, showed enhanced cellular responses to a chitin elicitor N-acetylchitoheptaose and increased resistance to the rice blast fungus Magnaporthe oryzae. Here, we investigated whether CEBiP fused with another type of receptor-like protein kinase (RLK) also functions as a chimeric receptor. Fusion proteins CRPis consist of CEBiP and the intracellular protein kinase region of a true resistance gene Pi-d2. Transgenic rice expressing a CRPi showed enhanced cellular responses specifically to N-acetylchitoheptaose in cultured cells and increased levels of disease resistance against M. oryzae in plants. These responses depended on the amino acid sequences predicted to be essential for the protein kinase activity of CRPi. The structure of the transmembrane domain in CRPi affected the protein accumulation, cellular responses, and disease resistance in transgenic rice. These results suggest that the chimeric receptor consisting of CEBiP and Pi-d2 functions as a receptor for chitin oligosaccharides and CEBiP-based chimeric receptors fused with other RLKs may also act as functional receptors.

Original languageEnglish
Pages (from-to)287-295
Number of pages9
JournalPlant Molecular Biology
Volume81
Issue number3
DOIs
Publication statusPublished - 2013
Externally publishedYes

Fingerprint

Magnaporthe
Magnaporthe oryzae
Disease Resistance
Chitin
chitin
protein kinases
disease resistance
rice
receptors
Protein Kinases
Oligosaccharides
genetically modified organisms
carbohydrate binding
blast disease
elicitors
protein kinase D2
Oryza
blight
oligosaccharides
cultured cells

Keywords

  • Chimeric receptor
  • Chitin
  • Disease resistance
  • Magnaporthe oryzae
  • MAMPs
  • Rice

ASJC Scopus subject areas

  • Plant Science
  • Agronomy and Crop Science
  • Genetics

Cite this

Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice. / Kouzai, Yusuke; Kaku, Hanae; Shibuya, Naoto; Minami, Eiichi; Nishizawa, Yoko.

In: Plant Molecular Biology, Vol. 81, No. 3, 2013, p. 287-295.

Research output: Contribution to journalArticle

@article{6844cc8be5d84469b3ceb202ad3771ad,
title = "Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice",
abstract = "We previously reported that rice plants expressing the chimeric receptor consisting of rice chitin oligosaccharides binding protein (CEBiP) and the intracellular protein kinase region of Xa21, which confers resistance to rice bacterial blight, showed enhanced cellular responses to a chitin elicitor N-acetylchitoheptaose and increased resistance to the rice blast fungus Magnaporthe oryzae. Here, we investigated whether CEBiP fused with another type of receptor-like protein kinase (RLK) also functions as a chimeric receptor. Fusion proteins CRPis consist of CEBiP and the intracellular protein kinase region of a true resistance gene Pi-d2. Transgenic rice expressing a CRPi showed enhanced cellular responses specifically to N-acetylchitoheptaose in cultured cells and increased levels of disease resistance against M. oryzae in plants. These responses depended on the amino acid sequences predicted to be essential for the protein kinase activity of CRPi. The structure of the transmembrane domain in CRPi affected the protein accumulation, cellular responses, and disease resistance in transgenic rice. These results suggest that the chimeric receptor consisting of CEBiP and Pi-d2 functions as a receptor for chitin oligosaccharides and CEBiP-based chimeric receptors fused with other RLKs may also act as functional receptors.",
keywords = "Chimeric receptor, Chitin, Disease resistance, Magnaporthe oryzae, MAMPs, Rice",
author = "Yusuke Kouzai and Hanae Kaku and Naoto Shibuya and Eiichi Minami and Yoko Nishizawa",
year = "2013",
doi = "10.1007/s11103-012-9998-7",
language = "English",
volume = "81",
pages = "287--295",
journal = "Plant Molecular Biology",
issn = "0167-4412",
publisher = "Springer Netherlands",
number = "3",

}

TY - JOUR

T1 - Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice

AU - Kouzai, Yusuke

AU - Kaku, Hanae

AU - Shibuya, Naoto

AU - Minami, Eiichi

AU - Nishizawa, Yoko

PY - 2013

Y1 - 2013

N2 - We previously reported that rice plants expressing the chimeric receptor consisting of rice chitin oligosaccharides binding protein (CEBiP) and the intracellular protein kinase region of Xa21, which confers resistance to rice bacterial blight, showed enhanced cellular responses to a chitin elicitor N-acetylchitoheptaose and increased resistance to the rice blast fungus Magnaporthe oryzae. Here, we investigated whether CEBiP fused with another type of receptor-like protein kinase (RLK) also functions as a chimeric receptor. Fusion proteins CRPis consist of CEBiP and the intracellular protein kinase region of a true resistance gene Pi-d2. Transgenic rice expressing a CRPi showed enhanced cellular responses specifically to N-acetylchitoheptaose in cultured cells and increased levels of disease resistance against M. oryzae in plants. These responses depended on the amino acid sequences predicted to be essential for the protein kinase activity of CRPi. The structure of the transmembrane domain in CRPi affected the protein accumulation, cellular responses, and disease resistance in transgenic rice. These results suggest that the chimeric receptor consisting of CEBiP and Pi-d2 functions as a receptor for chitin oligosaccharides and CEBiP-based chimeric receptors fused with other RLKs may also act as functional receptors.

AB - We previously reported that rice plants expressing the chimeric receptor consisting of rice chitin oligosaccharides binding protein (CEBiP) and the intracellular protein kinase region of Xa21, which confers resistance to rice bacterial blight, showed enhanced cellular responses to a chitin elicitor N-acetylchitoheptaose and increased resistance to the rice blast fungus Magnaporthe oryzae. Here, we investigated whether CEBiP fused with another type of receptor-like protein kinase (RLK) also functions as a chimeric receptor. Fusion proteins CRPis consist of CEBiP and the intracellular protein kinase region of a true resistance gene Pi-d2. Transgenic rice expressing a CRPi showed enhanced cellular responses specifically to N-acetylchitoheptaose in cultured cells and increased levels of disease resistance against M. oryzae in plants. These responses depended on the amino acid sequences predicted to be essential for the protein kinase activity of CRPi. The structure of the transmembrane domain in CRPi affected the protein accumulation, cellular responses, and disease resistance in transgenic rice. These results suggest that the chimeric receptor consisting of CEBiP and Pi-d2 functions as a receptor for chitin oligosaccharides and CEBiP-based chimeric receptors fused with other RLKs may also act as functional receptors.

KW - Chimeric receptor

KW - Chitin

KW - Disease resistance

KW - Magnaporthe oryzae

KW - MAMPs

KW - Rice

UR - http://www.scopus.com/inward/record.url?scp=84872601532&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84872601532&partnerID=8YFLogxK

U2 - 10.1007/s11103-012-9998-7

DO - 10.1007/s11103-012-9998-7

M3 - Article

C2 - 23242918

AN - SCOPUS:84872601532

VL - 81

SP - 287

EP - 295

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 3

ER -