Which amino acids can be Sumoylated?
Lysine is one of 20 common amino acids. Because of its physical and chemical properties, it can interact with several proteins or substrates. With respect to PTM, lysine is not only the most frequently modified amino acid but also the one subjected to the widest range of PTMs, which include SUMOylation.
What is the role of SUMOylation?
SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases.
What is SUMOylation process?
SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle. In contrast to ubiquitin, SUMO is not used to tag proteins for degradation.
What are the effects of SUMOylation?
Ubiquitin and Ubiquitin-like Protein Modifiers SUMOylation generally impacts protein–protein interactions and the assembly of multiprotein complexes. Cellular processes regulated by SUMOylation include DNA damage responses, cell cycle progression, or the control of gene expression.
What is SUMO tag used for?
SUMO Tag Definition Sumo tag is most frequently used as N-end fusion sequence in yeast to increase the expression and solubility of the desired recombinant protein. SUMO proteins are similar to ubiquitin in their folded structure but possess only about 20% homology to the amino acid sequence of ubiquitin.
What is a sumo ligase?
Often referred to as a protein ligase, an E3 enzyme either facilitates transfer of ubiquitin or ubiquitin-like proteins (including SUMO) from the E2 conjugating enzyme to a substrate or catalyzes thioester bond transfer between the E2 and E3 Cys before substrate conjugation, as is the case for HECT E3s.
What is SUMO tag?
Who discovered SUMOylation?
Fifteen years ago, molecular biologist Frauke Melchior discovered a new mechanism of posttranslational protein modification that controls a variety of processes in eukaryotic cells.
How does SUMO tag increase solubility?
SUMO-tag gene fusion acts as both a chaperonin and as an initiator of protein folding in both prokaryotic and eukaryotic systems. Addition of this tag enables protein experts to increase the expression levels of recombinant proteins and to significantly improve protein solubility.
What are ubiquitin and SUMO and what is their general purpose?
Ubiquitin (Ub, top pathway) and SUMO (S, bottom), known as modifiers, are small polypeptides that are usually conjugated to internal lysine residues of target proteins through their C-terminal glycine residues, forming isopeptide bonds. Both modifications are reversible.
What is sumoylation of lysine residues?
SUMOylation is a reversible PTM in which small ubiquitin-like modifier (SUMO) proteins are covalently attached to lysine residues, in a process similar to ubiquitylation. Modification of substrate protein by SUMO is referred to as sumoylation. The first substrate for sumoylation to be identified was RanGAP1, a GTPase-activating protein.
What is sumoylation of amino acids?
Sumoylation consists in the addition of a “Small Ubiquitin-related MOdifier protein” (SUMO) of ~100 amino acids. Similar to ubiquitination, SUMO is always covalently attached to other proteins through the activities of members of an enzymatic cascade (E1-E2-E3).
What are SUMO proteins?
Small Ubiquitin-like Modifier (or SUMO) proteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function.
What is the effect of sumoylation on target proteins?
SUMOylation of target proteins has been shown to cause a number of different outcomes including altered localization and binding partners. The SUMO-1 modification of RanGAP1 (the first identified SUMO substrate) leads to its trafficking from cytosol to nuclear pore complex.