Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.

CORONATINE INSENSITIVE 1 (COI1) encodes an E3 ubiquitin ligase complex component that interacts with JAZ proteins and targets them for degradation in response to JA signaling. The Arabidopsis genome has a single copy of COI1, but the Oryza sativa genome has three closely related COI homologs. To exa...

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Main Authors: Han Yong Lee, Ju-Seok Seo, Jang Hee Cho, Harin Jung, Ju-Kon Kim, Jong Seob Lee, Sangkee Rhee, Yang Do Choi
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3540053?pdf=render
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spelling doaj-f91b72e0831a479eb4a8cbc392a555382020-11-25T00:44:18ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0181e5280210.1371/journal.pone.0052802Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.Han Yong LeeJu-Seok SeoJang Hee ChoHarin JungJu-Kon KimJong Seob LeeSangkee RheeYang Do ChoiCORONATINE INSENSITIVE 1 (COI1) encodes an E3 ubiquitin ligase complex component that interacts with JAZ proteins and targets them for degradation in response to JA signaling. The Arabidopsis genome has a single copy of COI1, but the Oryza sativa genome has three closely related COI homologs. To examine the functions of the three OsCOIs, we used yeast two-hybrid assays to examine their interactions with JAZ proteins and found that OsCOIs interacted with OsJAZs and with JAZs, in a coronatine dependent manner. We also tested whether OsCOI1a and OsCOI1b could complement Arabidopsis coi1-1 mutants and found that overexpression of either gene in the coi1-1 mutant resulted in restoration of JA signal transduction and production of seeds, indicating successful complementation. Although OsCOI2 interacted with a few OsJAZs, we were not able to successfully complement the coi1-1 mutant with OsCOI2. Molecular modeling revealed that the three OsCOIs adopt 3D structures similar to COI1. Structural differences resulting from amino acid variations, especially among amino acid residues involved in the interaction with coronatine and JAZ proteins, were tested by mutation analysis. When His-391 in OsCOI2 was substituted with Tyr-391, OsCOI2 interacted with a wider range of JAZ proteins, including OsJAZ1, 2, 5∼9 and 11, and complemented coi1-1 mutants at a higher frequency than the other OsCOIs and COI1. These results indicate that the three OsCOIs are orthologues of COI1 and play key roles in JA signaling.http://europepmc.org/articles/PMC3540053?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Han Yong Lee
Ju-Seok Seo
Jang Hee Cho
Harin Jung
Ju-Kon Kim
Jong Seob Lee
Sangkee Rhee
Yang Do Choi
spellingShingle Han Yong Lee
Ju-Seok Seo
Jang Hee Cho
Harin Jung
Ju-Kon Kim
Jong Seob Lee
Sangkee Rhee
Yang Do Choi
Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
PLoS ONE
author_facet Han Yong Lee
Ju-Seok Seo
Jang Hee Cho
Harin Jung
Ju-Kon Kim
Jong Seob Lee
Sangkee Rhee
Yang Do Choi
author_sort Han Yong Lee
title Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
title_short Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
title_full Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
title_fullStr Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
title_full_unstemmed Oryza sativa COI homologues restore jasmonate signal transduction in Arabidopsis coi1-1 mutants.
title_sort oryza sativa coi homologues restore jasmonate signal transduction in arabidopsis coi1-1 mutants.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description CORONATINE INSENSITIVE 1 (COI1) encodes an E3 ubiquitin ligase complex component that interacts with JAZ proteins and targets them for degradation in response to JA signaling. The Arabidopsis genome has a single copy of COI1, but the Oryza sativa genome has three closely related COI homologs. To examine the functions of the three OsCOIs, we used yeast two-hybrid assays to examine their interactions with JAZ proteins and found that OsCOIs interacted with OsJAZs and with JAZs, in a coronatine dependent manner. We also tested whether OsCOI1a and OsCOI1b could complement Arabidopsis coi1-1 mutants and found that overexpression of either gene in the coi1-1 mutant resulted in restoration of JA signal transduction and production of seeds, indicating successful complementation. Although OsCOI2 interacted with a few OsJAZs, we were not able to successfully complement the coi1-1 mutant with OsCOI2. Molecular modeling revealed that the three OsCOIs adopt 3D structures similar to COI1. Structural differences resulting from amino acid variations, especially among amino acid residues involved in the interaction with coronatine and JAZ proteins, were tested by mutation analysis. When His-391 in OsCOI2 was substituted with Tyr-391, OsCOI2 interacted with a wider range of JAZ proteins, including OsJAZ1, 2, 5∼9 and 11, and complemented coi1-1 mutants at a higher frequency than the other OsCOIs and COI1. These results indicate that the three OsCOIs are orthologues of COI1 and play key roles in JA signaling.
url http://europepmc.org/articles/PMC3540053?pdf=render
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