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

• Published in: PloS one Vol. 15; no. 3; p. e0230177
• Main Authors: Wang, Peng, Yu, Shuojun, Han, Xiaokang, Xu, Junya, He, Qingyuan, Xu, Sheng, Wang, Ren
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 17.03.2020; Public Library of Science (PLoS)
• Subjects: Alkaloids; Amaryllidaceae; Biology and Life Sciences; Biosynthesis; Characterization; Cloning; Cytoplasm; Displays (Marketing); EDTA; Enzymes; Flowers & plants; Gene expression; Genes; Genetic aspects; Genetic engineering; Germplasm; Gibberellins; Jasmonic acid; Localization; Lycoris aurea; Maximum likelihood method; Meristems; Metabolism; Metabolites; Methyl jasmonate; Nuclei (cytology); Phylogenetics; Physical Sciences; Physiological aspects; Plant growth; Plant hormones; Plant metabolites; Plant sciences; Polymerase chain reaction; Proteins; Regulatory mechanisms (biology); Research and Analysis Methods; Reverse transcription; Secondary metabolites; Signal processing; Transcription (Genetics); Zinc finger proteins; China; Beijing China
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0230177

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.