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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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 |
work_keys_str_mv |
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