A Maize Jasmonate Zim-Domain Protein, ZmJAZ14, Associates with the JA, ABA, and GA Signaling Pathways in Transgenic Arabidopsis

Zhou, Xiaojin; Yan, Shengwei; Sun, Cheng; Li, Suzhen; Li, Jie; Xu, Miaoyun; Liu, Xiaoqing; Zhang, Shaojun; Zhao, Qianqian; Li, Ye; Fan, Yanting; Chen, Rumei; Wang, Lei

doi:10.1371/journal.pone.0121824

Cited by 42 publications

(40 citation statements)

References 66 publications

(84 reference statements)

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“…Such differential expression patterns suggest that the transcription of these seven LaJAZ genes would subject to different regulatory mechanisms in L. aurea tissues. Similarly, previous studies also indicated that JAZ genes are differentially and constitutively expressed in different plant species such as rice [15], cotton [47], maize [48], rubber tree [49] and sugarcane [50]. Moreover, JAZ genes could be significantly induced by MeJA treatment [17,47,50,51].…”

Section: Plos Onementioning

confidence: 65%

Identification, molecular characterization and expression of JAZ genes in Lycoris aurea

Wang

Han

et al. 2020

PLoS ONE

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Jasmonates (JAs) are key phytohormones involved in regulation of plant growth and development, stress responses, and secondary metabolism. It has been reported that treatments with JAs could increase the contents of Amaryllidaceae alkaloids in Amaryllidaceae plants. Jasmonate ZIM (zinc-finger inflorescence meristem) domain (JAZ) proteins are key components in JA signal processes. However, JAZ proteins have not been characterized in genus Lycoris. In this study, we identified and cloned seven differentially expressed JAZ genes (namely LaJAZ1-LaJAZ7) from Lycoris aurea. Bioinformatic analyses revealed that these seven LaJAZ proteins contain the ZIM domain and JA-associated (Jas, also named CCT_2) motif. Quantitative reverse transcription polymerase chain reaction (qRT-PCR) analysis revealed that these LaJAZ genes display different expression patterns in L. aurea tissues, and most of them are inducible when treated with methyl jasmonate (MeJA) treatment. Subcellular localization assay demonstrated that LaJAZ proteins are localized in the cell nucleus or cytoplasm. In addition, LaJAZ proteins could interact with each other to form homodimer and/or heterodimer. The findings in this study may facilitate further functional research of the LaJAZ genes, especially the potential regulatory mechanism of plant secondary metabolites including Amaryllidaceae alkaloids in L. aurea.

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Section: Plos Onementioning

confidence: 65%

Identification, molecular characterization and expression of JAZ genes in Lycoris aurea

Wang

Han

et al. 2020

PLoS ONE

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“…As a typical JAZ protein, GhJAZ2 contains a ZIM domain and a C‐terminal Jas domain, interacts with GhCOI1 and can be degraded by exogenous MeJA (Figs and S1C). Although the Jas domain has been proposed to play an important role in the degradation of JAZ proteins, increasingly, reports have shown that the overexpression of JAZ can repress JA signalling whether or not it contains the Jas domain (Yang et al ., ; Zhou et al ., ). Overexpression of GhJAZ2 reduces the sensitivity to JA in cotton and impairs the resistance to V. dahliae and insect herbivory, in spite of the instability of GhJAZ2 in cells containing high levels of JAs (Figs , 2 and S2).…”

Section: Discussionmentioning

confidence: 97%

“…As a typical JAZ protein, GhJAZ2 contains a ZIM domain and a C-terminal Jas domain, interacts with GhCOI1 and can be degraded by exogenous MeJA (Figs 3 and S1C). Although the Jas domain has been proposed to play an important role in the degradation of JAZ proteins, increasingly, reports have shown that the overexpression of JAZ can repress JA signalling whether or not it contains the Jas domain Zhou et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

GhJAZ2 attenuates cotton resistance to biotic stresses via the inhibition of the transcriptional activity of GhbHLH171

Zhu

et al. 2017

Molecular Plant Pathology

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Plants have evolved effective mechanisms to protect themselves against multiple stresses, and employ jasmonates (JAs) as vital defence signals to defend against pathogen infection. The accumulation of JA, induced by signals from biotic and abiotic stresses, results in the degradation of Jasmonate-ZIM-domain (JAZ) proteins, followed by the de-repression of JAZ-repressed transcription factors (such as MYC2) to activate defence responses and developmental processes. Here, we characterized a JAZ family protein, GhJAZ2, from cotton (Gossypium hirsutum) which was induced by methyl jasmonate (MeJA) and inoculation of Verticillium dahliae. The overexpression of GhJAZ2 in cotton impairs the sensitivity to JA, decreases the expression level of JA-response genes (GhPDF1.2 and GhVSP) and enhances the susceptibility to V. dahliae and insect herbivory. Yeast two-hybrid and bimolecular fluorescence complementation assays showed that GhJAZ2 may be involved in the regulation of cotton disease resistance by interaction with further disease-response proteins, such as pathogenesis-related protein GhPR10, dirigent-like protein GhD2, nucleotide-binding site leucine-rich repeat (NBS-LRR) disease-resistant protein GhR1 and a basic helix-loop-helix transcription factor GhbHLH171. Unlike MYC2, overexpression of GhbHLH171 in cotton activates the JA synthesis and signalling pathway, and improves plant tolerance to the fungus V. dahliae. Molecular and genetic evidence shows that GhJAZ2 can interact with GhbHLH171 and inhibit its transcriptional activity and, as a result, can restrain the JA-mediated defence response. This study provides new insights into the molecular mechanisms of GhJAZ2 in the regulation of the cotton defence response.

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“…TIFY family proteins can be classified into 4 subfamilies based on their constituent domains [ 40 ]: TIFY subfamily, containing only the TIFY (ZIM) domain; ZML (ZIM-like) subfamily, containing the TIFY, CCT and ZML domains; JAZ subfamily, containing the TIFY and Jas domains (also called the CCT_2 domain); and PPD subfamily, containing the TIFY domain and a truncated Jas domain. The TIFY family plays a role in regulating diverse biological processes in plants, including elongation of the petiole and hypocotyls [ 42 ], root growth [ 43 ], flower abscission [ 44 ], leaf development [ 45 ] and responses to abiotic and biotic stress [ 46 – 48 ].…”

Section: Discussionmentioning

confidence: 99%

A JAZ Protein in Astragalus sinicus Interacts with a Leghemoglobin through the TIFY Domain and Is Involved in Nodule Development and Nitrogen Fixation

Wang

et al. 2015

PLoS ONE

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Leghemoglobins (Lbs) play an important role in legumes-rhizobia symbiosis. Lbs bind O2 and protect nitrogenase activity from damage by O2 in nodules, therefore, they are regarded as a marker of active nitrogen fixation in nodules. Additionally, Lbs are involved in the nitric oxide (NO) signaling pathway, acting as a NO scavenger during nodule development and nitrogen fixation. However, regulators responsible for Lb expression and modulation of Lb activity have not been characterized. In our previous work, a Jasmonate-Zim-domain (JAZ) protein interacting with a Lb (AsB2510) in Astragalus sinicus was identified and designated AsJAZ1. In this study, the interaction between AsJAZ1 and AsB2510 was verified using a yeast two-hybrid system and in vitro Glutathione S-transferase (GST) pull-down assays, resulting in identification of the interaction domain as a TIFY (previously known as zinc-finger protein expressed in inflorescence meristem, ZIM) domain. TIFY domain is named after the most conserved amino acids within the domain. Bimolecular fluorescence complementation (BiFC) was used to confirm the interaction between AsJAZ1 and AsB2510 in tobacco cells, demonstrating that AsJAZ1-AsB2510 interaction was localized to the cell membrane and cytoplasm. Furthermore, the expression patterns and the symbiotic phenotypes of AsJAZ1 were investigated. Knockdown of AsJAZ1 expression via RNA interference led to decreased number of nodules, abnormal development of bacteroids, accumulation of poly-x-hydroxybutyrate (PHB) and loss of nitrogenase activity. Taken together, our results suggest that AsJAZ1 interacts with AsB2510 and participates in nodule development and nitrogen fixation. Our results provide novel insights into the functions of Lbs or JAZ proteins during legume-rhizobia symbiosis.

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A Maize Jasmonate Zim-Domain Protein, ZmJAZ14, Associates with the JA, ABA, and GA Signaling Pathways in Transgenic Arabidopsis

Cited by 42 publications

References 66 publications

Identification, molecular characterization and expression of JAZ genes in Lycoris aurea

Identification, molecular characterization and expression of JAZ genes in Lycoris aurea

GhJAZ2 attenuates cotton resistance to biotic stresses via the inhibition of the transcriptional activity of GhbHLH171

A JAZ Protein in Astragalus sinicus Interacts with a Leghemoglobin through the TIFY Domain and Is Involved in Nodule Development and Nitrogen Fixation

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