BiFC-SUMO:a large-scale strategy for screening human SUMOylation modification and SUMO non-covalent binding substrates
Small ubiquitin-related modification(SUMO)is a type of post-translational modifications that plays a crucial role in various biological and pathological processes.SUMO proteins can interact with target proteins with covalent and non-covalent bonds,known as SUMOylation and SUMO non-covalent binding.While most studies focused on covalent SUMOylation,SUMO binding with weak and transient nature,especially simultaneous detection of both SUMOylation and SUMO binding was still lacking.To overcome this limitation,we developed a high-throughput simultaneous identification method for both SUMOylation and SUMO binding target proteins based on the bimolecular fluorescence complementation experiment and deep learning algorithm DeepSUMO.By utilizing this approach,we successfully identified 1379 non-covalent and 8457 covalent SUMO regulatory proteins,with over 70％being identified for the first time.Our findings highlight the critical role of SUMO regulation and may provide valuable resource for future research on both covalent and non-covalent SUMO modification.DeepSUMO is now available as an online service(http://deepsumo.renlab.org)for public use.
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