Abstract
Jasmonate ZIM-domain (JAZ) family proteins are the key repressors in the jasmonate signaling pathway and play crucial roles in plant development, defenses, and responses to stresses. However, our knowledge about the JAZ protein family in petunia is limited. This research respectively identified 12 and 16 JAZ proteins in two Petunia progenitors, Petunia axillaris and Petunia inflata. Phylogenetic analysis showed that the 28 proteins could be divided into four groups (Groups A–D) and further classified into six subgroups (A1, A2, B1, B3, C, and D1); members in the same subgroup shared some similarities in motif composition and sequence structure. The Ka/Ks ratios of seven paralogous pairs were less than one, suggesting the petunia JAZ family might have principally undergone purifying selection. Quantitative real-time PCR (qRT-PCR) analysis revealed that PaJAZ genes presented differential expression patterns during the development of flower bud and anther in petunia, and the expression of PaJAZ5, 9, 12 genes was generally up-regulated after MeJA treatment. Subcellular localization assays demonstrated that proteins PaJAZ5, 9, 12 were localized in nucleus. Yeast two hybrid (Y2H) elucidated most PaJAZ proteins (PaJAZ1-7, 9, 12) might interact with transcription factor MYC2. This study provides insights for further investigation of functional analysis in petunia JAZ family proteins.
Highlights
The oxylipin-derived phytohormone jasmonate (JA) regulates growth, development, secondary metabolism, and stress responses during the plant life cycle [1,2,3,4,5,6]
16 Jasmonate ZIM-domain (JAZ) proteins were identified in P. axillaris and P. inflata genomes
They were respectively designated as PaJAZ1-12 and PiJAZ1-16 according to the naming convention (Table 1)
Summary
The oxylipin-derived phytohormone jasmonate (JA) regulates growth, development, secondary metabolism, and stress responses during the plant life cycle [1,2,3,4,5,6]. The (+)-7-iso-Jasmonoyl-L-isoleucine (JA-Ile), which has a structure greatly similar to coronatine, is the endogenous bioactive form of the hormone [7], and the biosynthesis of JA-Ile relies on the reduction of 12-oxo-phytodienoic acid (OPDA), the JA precursor, which can be reduced by OPDA reductase 3 (OPR3) [2]. An OPR3-independent pathway to synthesize bioactive JA was discovered. Previous research elucidated that JAZ proteins, as the repressors, could play crucial roles in JA signaling pathways [9,10,11]. Without the JA stimulation, TOPLESS (TPL) or TPL-related proteins (TRPs) could be recruited by JAZ proteins via the adapter protein NINJA to form the co-repressors complex [12] and further interact with a variety of downstream transcription factors to suppress diverse
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