Identification, characterization and putative function of HvRin4, a barley homolog of Arabidopsis Rin4

Upinder Gill; Jayaveeramuthu Nirmala; Robert Brueggeman; Andris Kleinhofs

doi:10.1016/j.pmpp.2012.08.002

Identification, characterization and putative function of HvRin4, a barley homolog of Arabidopsis Rin4

Upinder Gill, Jayaveeramuthu Nirmala, Robert Brueggeman, Andris Kleinhofs

Veterinary Population Medicine

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

RIN4 is a signaling molecule that plays a key role in disease resistance responses in plants. Barley RIN4 (HvRIN4) was first identified as an interactor of the stem rust resistance protein RPG1 in a yeast two-hybrid system. Therefore, we isolated, characterized and studied HvRIN4 role in barley. Yeast two hybrid analysis, employing several deletion mutants of HvRIN4 revealed that the C-terminal end and a partial deletion of N-terminal end of HvRIN4 are important for interacting with RPG1. HvRIN4 interactions with RPG1 mutated proteins, which inactivate autophosphorylation, suggested that autophosphorylation or the amino acids required for autophosphorylation of RPG1 are essential for interaction.

Original language	English (US)
Pages (from-to)	41-49
Number of pages	9
Journal	Physiological and Molecular Plant Pathology
Volume	80
DOIs	https://doi.org/10.1016/j.pmpp.2012.08.002
State	Published - Oct 2012

Bibliographical note

Funding Information:
Research was supported by National Research Initiative of the United States Department of Agriculture Co-operative State Research, Education, and Extension Service Grant No. 2007-35301-18205 to A.K and B.J.S.

Keywords

Disease resistance
HvRin4
Protein-protein interactions
RPG1
Stem rust
Virus induced gene silencing (VIGS)

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10.1016/j.pmpp.2012.08.002

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title = "Identification, characterization and putative function of HvRin4, a barley homolog of Arabidopsis Rin4",

abstract = "RIN4 is a signaling molecule that plays a key role in disease resistance responses in plants. Barley RIN4 (HvRIN4) was first identified as an interactor of the stem rust resistance protein RPG1 in a yeast two-hybrid system. Therefore, we isolated, characterized and studied HvRIN4 role in barley. Yeast two hybrid analysis, employing several deletion mutants of HvRIN4 revealed that the C-terminal end and a partial deletion of N-terminal end of HvRIN4 are important for interacting with RPG1. HvRIN4 interactions with RPG1 mutated proteins, which inactivate autophosphorylation, suggested that autophosphorylation or the amino acids required for autophosphorylation of RPG1 are essential for interaction.",

keywords = "Disease resistance, HvRin4, Protein-protein interactions, RPG1, Stem rust, Virus induced gene silencing (VIGS)",

author = "Upinder Gill and Jayaveeramuthu Nirmala and Robert Brueggeman and Andris Kleinhofs",

note = "Funding Information: Research was supported by National Research Initiative of the United States Department of Agriculture Co-operative State Research, Education, and Extension Service Grant No. 2007-35301-18205 to A.K and B.J.S.",

year = "2012",

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doi = "10.1016/j.pmpp.2012.08.002",

language = "English (US)",

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AU - Gill, Upinder

AU - Nirmala, Jayaveeramuthu

AU - Brueggeman, Robert

AU - Kleinhofs, Andris

N1 - Funding Information: Research was supported by National Research Initiative of the United States Department of Agriculture Co-operative State Research, Education, and Extension Service Grant No. 2007-35301-18205 to A.K and B.J.S.

PY - 2012/10

Y1 - 2012/10

N2 - RIN4 is a signaling molecule that plays a key role in disease resistance responses in plants. Barley RIN4 (HvRIN4) was first identified as an interactor of the stem rust resistance protein RPG1 in a yeast two-hybrid system. Therefore, we isolated, characterized and studied HvRIN4 role in barley. Yeast two hybrid analysis, employing several deletion mutants of HvRIN4 revealed that the C-terminal end and a partial deletion of N-terminal end of HvRIN4 are important for interacting with RPG1. HvRIN4 interactions with RPG1 mutated proteins, which inactivate autophosphorylation, suggested that autophosphorylation or the amino acids required for autophosphorylation of RPG1 are essential for interaction.

AB - RIN4 is a signaling molecule that plays a key role in disease resistance responses in plants. Barley RIN4 (HvRIN4) was first identified as an interactor of the stem rust resistance protein RPG1 in a yeast two-hybrid system. Therefore, we isolated, characterized and studied HvRIN4 role in barley. Yeast two hybrid analysis, employing several deletion mutants of HvRIN4 revealed that the C-terminal end and a partial deletion of N-terminal end of HvRIN4 are important for interacting with RPG1. HvRIN4 interactions with RPG1 mutated proteins, which inactivate autophosphorylation, suggested that autophosphorylation or the amino acids required for autophosphorylation of RPG1 are essential for interaction.

KW - Disease resistance

KW - HvRin4

KW - Protein-protein interactions

KW - RPG1

KW - Stem rust

KW - Virus induced gene silencing (VIGS)

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JO - Physiological and Molecular Plant Pathology

JF - Physiological and Molecular Plant Pathology

ER -

Identification, characterization and putative function of HvRin4, a barley homolog of Arabidopsis Rin4

Abstract

Bibliographical note

Keywords

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