Recent in vivo experiments have shown that the UVR8 C-terminal region (aa 397–423 UVR8 C27) alone is sufficient to regulate the activity of COP1. In the monomeric form, UVR8 binds the E3 ubiquitin ligase COP1 (CONSTITUTIVELY PHOTOMORPHOGENIC 1), triggering subsequent UV-B-dependent photomorphogenic development in plants. Upon absorption of UV radiation, the protein monomerizes into its photoactivated state. UVR8 is a homodimer in its signalling inactive form. We also integrated histone modifications into our RF model, which demonstrated H3K36me3 and H3K27me3 as determining features for m6A distribution.UVR8 (UV RESISTANCE LOCUS 8) is a UV-B photoreceptor responsible for initiating UV-B signalling in plants. Specific RBPs can engage to the corresponding regional m6A sites and deploy distinct regulatory processes, such as cleavage site selection of the alternative polyadenylation (APA). The RF model exhibited fairly high prediction accuracy across cell lines, suggesting a conservative RBP interaction network regulates m6A occupancy. Redundancy analysis showed that several RBPs may have similar binding patterns with m6A sites. The relative importance of different RBPs from the model provided a quantitative metric to evaluate their interactions with m6A modifications. Accurate prediction of m6A sites demonstrated significant connections between RBP bindings and m6A modifications. We designed a Random Forest (RF) model to systematically analyze the interaction among RBPs and m6A modifications by integrating the binding signals from hundreds of RBPs. RNA-binding proteins (RBPs) have critical roles in N6-methyladenosine (m6A) modification process.
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