Be mediated by the higher levels of JAZ7 titrating out transcriptional repressors which include JAM1. JAM1, JAM2 and JAM3 bind exactly the same DNA motif (G-box, CACGTG) as MYC2, MYC3 and MYC4 (Nakata et al., 2013; Fonseca et al., 2014), and by means of competitive binding for the exact same DNA-binding web page, these transcriptional repressors and activators can fine-tune JA-mediated responses. An unbiased in silico search (TAIR motif evaluation: Statistical Motif Analysis in Promoter or Upstream Gene Sequences, 1000 bp) for G-box motifs (Dombrecht et al., 2007; Fernandez-Calvo et al., 2011) within the promoters in the up-regulated genes in jaz7-1D (Supplementary Table S5) identified 19 to contain the CACGTG G-box motif, and2384 | Thatcher et al.and 38 to include the MYC2 binding variants Ro 32-0432 (hydrochloride) Epigenetic Reader Domain CACATG and CACGTT, respectively (Dombrecht et al., 2007). The promoters of down-regulated jaz7-1D (Supplementary Table S6) genes also contained these motifs (CACGTG: 7; CACATG: 8; CACGTT: 4). These findings suggest JAZ7 co-ordinates the expression of stress-responsive genes by way of its interaction with specific MYC or JAM transcription factors and their binding to G-box DNA motifs. The ZIM domain of JAZ proteins mediates their homo- or heterodimerization (Chini et al., 2009; Chung and Howe, 2009; Chung et al., 2009), but JAZ7 appears to be the only JAZ protein incapable of homodimerizing or forming heterodimers with other JAZ proteins (Chini et al., 2009; Chung and Howe, 2009; reviewed by Pauwels and Goossens, 2011). One more TIFYcontaining protein not capable of interacting with JAZ proteins may be the non-JAZ protein TIFY8 (Cu lar P ez et al., 2014). While TIFY8 has a functional ZIM domain that mediates transcriptional repression by recruiting TPL by means of NINJA, its ZIM domain will not confer interactions with JAZ proteins. The differences in JAZ7 protein-protein interactions suggest JAZ7 will not function like the other JAZ repressors. Further to this, despite the fact that Jas and ZIM motifs in JAZ7 and JAZ8 are related, suggestive of comparable binding activity (Shyu et al., 2012; Wager and Browse, 2012), they regulate binding to diverse transcription elements. For example, we identified JAZ7 and JAZ8 interacted with MYC34 and JAM1, but only JAZ8 interacted with MYC2. JAZ8 but not JAZ7, also interacts with JAM2 (Song et al., 2013; Fonseca et al., 2014), with two regulators of stamen improvement (MYB21 and MYB24) (Song et al., 2011) and with WD-repeatbHLHMYB complicated members that regulate anthocyanin biosynthesis and trichome initiation (EGL3, GL3, TT8, MYB75, GL1, TTG1) (Qi et al., 2011). These differences in transcription factor binding could explain why JAZ8 overexpression confers reduced JA-sensitivity (Shyu et al., 2012) when high levels of JAZ7 in jaz7-1D plants confers elevated JA-sensitivity (this function). In summary, our final results help a model in which F. oxysporum stimulates JA-signaling, resulting in increased JAZ7 expression and JAZ7-TPL-mediated repression contributing towards the control of JA-responses and illness progression. Our characterization with the jaz7-1D mutant suggests the ectopic or ETYA Cancer non-wild-type higher levels of JAZ7 in jaz7-1D is really a key determinant of its phenotypes and that these abnormal levels may be detrimental for the standard COI1-JAZ-TPL-MYCJAM regulatory network top to hyperactivation of JA-signaling (Fig. 14B). In addition, the uncommon protein binding properties of JAZ7 when compared with other JAZs may possibly exacerbate this phenotype (e.g. lack of homo- or heterodimerization, dive.
