GmHSP40.1, a nuclear-localized soybean J domain protein, participates in regulation of flowering time through interacting with EMF1 and JMJ14

Heat shock protein 40s (HSP40s) are a group of J domain proteins (JDPs), which serve as co-chaperones for heat shock protein 70s. We previously reported that over-expression of a soybean class C JDP, GmHSP40.1, in Arabidopsis activated defense responses. Surprisingly, a significantly delayed flowering phenotype was also observed for the GmHSP40.1-overexpressing (OE) lines. We provided evidence that the late-flowering phenotype observed in the GmHSP40.1-OE lines was not due to impaired pri-miRNA processing and pre-mRNA splicing. Instead, we found that GmHSP40.1 interacted and co-localized with both EMF1 and JMJ14, two major components in the EMF1 complex (EMF1c), which plays a key role in depositing and maintaining the H3K27me3 modification in the FT locus. Consistent with these interactions, the H3K27me3 modification at FT chromatin was significantly increased, whereas the H3K27me3 modification at FLC locus was significantly decreased in the GmHSP40.1-OE line compared with the wde-type Col-0. Interestingly, the H3K4me3 modification was just opposite to H3K27me3 modification at FT and FLC loci, suggesting an antagonistic relationship between these two modifications. Accordingly, the expression of FT and FLC was significantly reduced and increased, respectively, in the GmHSP40.1-OE line compared with that of Col-0. Lastly, we showed that both EMF1 and JMJ14 are genetically epistatic to GmHSP40.1-overexpression. Together, our results revealed that GmHSP40.1 negatively regulates flowering time through promoting the function of EMF1c via interacting with both EMF1 and JMJ14.