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Small Ubiquitin-Related Modifier 3 (SUMO3) is a member of the SUMO family of proteins, which are ubiquitin-like proteins involved in post-translational modification of other proteins. SUMOylation, the process of attaching SUMO proteins to target proteins, plays a crucial role in various cellular processes, including nuclear transport, transcriptional regulation, apoptosis, protein stability, response to stress, and cell cycle progression .
SUMO3, like other SUMO proteins, is covalently attached to target proteins via an isopeptide bond between the C-terminal glycine residue of SUMO3 and an acceptor lysine on the target protein . This modification can alter the localization, stability, and interaction partners of the target protein, thereby influencing its function .
SUMO3 is highly similar to SUMO2, with which it shares a high degree of sequence identity . Both SUMO2 and SUMO3 are distinct from SUMO1, another member of the SUMO family . SUMO3 is involved in various cellular processes, including nuclear transport, DNA replication and repair, mitosis, and signal transduction .
The SUMOylation process involves a cascade of enzymatic reactions similar to ubiquitination. It begins with the activation of SUMO3 by the E1 enzyme complex (SAE1-SAE2), followed by its conjugation to the E2 enzyme (UBE2I). The final step involves the transfer of SUMO3 to the target protein, which can be facilitated by E3 ligases such as PIAS1-4, RANBP2, or CBX4 .
SUMOylation is a reversible process, and the removal of SUMO3 from target proteins is mediated by deSUMOylating enzymes . This dynamic modification allows cells to rapidly respond to various stimuli and stress conditions. SUMO3 modification has been shown to regulate protein stability, nuclear-cytosolic transport, and transcriptional activity .
Human recombinant SUMO3 is widely used in research to study the SUMOylation process and its effects on target proteins. It is also used to investigate the role of SUMO3 in various cellular processes and diseases. Recombinant SUMO3 can be produced in large quantities using bacterial expression systems, making it a valuable tool for biochemical and structural studies.