Exploring potential roles for the interaction of MOM1 with SUMO and the SUMO E3 ligase-like protein PIAL2 in transcriptional silencing.

The CHD3-like chromatin remodeling protein MOM1 and the PIAS-type SUMO E3 ligase-like protein PIAL2 are known to interact with each other and mediate transcriptional silencing in Arabidopsis. However, it is poorly understood whether and how the interaction is involved in transcriptional silencing. Here, we demonstrate that, while the PIAL2 interaction domain (PIAL2-IND) is required for PIAL2 dimerization, MOM-PIAL2 interaction, and transcriptional silencing, a transgene fusing the wild-type MOM1 protein with the PIAL2 protein defective in PIAL2-IND can completely restore transcriptional silencing in the mom1/pial2 double mutant, demonstrating that the artificial fusion of MOM1 and PIAL2 mimics the in vivo interaction of these two proteins so that PIAL2-IND is no longer required for transcriptional silencing in the fusion protein. Further, our yeast two-hybrid assay identifies a previously unrecognized SUMO interaction motif (SIM) in the conserved MOM1 motif CMM3 and demonstrates that the SIM is responsible for the interaction of MOM1 with SUMO. Given that eukaryotic PIAS-type SUMO E3 ligases have a conserved role in chromatin regulation, the findings reported in this study may represent a conserved chromatin regulatory mechanism in higher eukaryotes.