Identification of a new small ubiquitin-like modifier (SUMO)-interacting motif in the E3 ligase PIASy
| Autor: | Hyewon Park, Nootan Pandey, Yoshiaki Azuma, Roberto N. De Guzman, Kawaljit Kaur |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular DNA repair Recombinant Fusion Proteins Amino Acid Motifs SUMO protein SUMO enzymes Xenopus Proteins Ligands Biochemistry 03 medical and health sciences Xenopus laevis Ubiquitin Animals Humans Protein inhibitor of activated STAT Protein Interaction Domains and Motifs Ligase activity Molecular Biology Ubiquitins biology Nitrogen Isotopes C-terminus Sumoylation Cell Biology Molecular biology Protein Inhibitors of Activated STAT Peptide Fragments Recombinant Proteins Ubiquitin ligase Cell biology Repressor Proteins 030104 developmental biology Protein Structure and Folding Mutation biology.protein Mutagenesis Site-Directed Small Ubiquitin-Related Modifier Proteins Hydrophobic and Hydrophilic Interactions Gene Deletion |
| Popis: | Small ubiquitin-like modifier (SUMO) conjugation is a reversible post-translational modification process implicated in the regulation of gene transcription, DNA repair, and cell cycle. SUMOylation depends on the sequential activities of E1 activating, E2 conjugating, and E3 ligating enzymes. SUMO E3 ligases enhance transfer of SUMO from the charged E2 enzyme to the substrate. We have previously identified PIASy, a member of the Siz/protein inhibitor of activated STAT (PIAS) RING family of SUMO E3 ligases, as essential for mitotic chromosomal SUMOylation in frog egg extracts and demonstrated that it can mediate effective SUMOylation. To address how PIASy catalyzes SUMOylation, we examined various truncations of PIASy for their ability to mediate SUMOylation. Using NMR chemical shift mapping and mutagenesis, we identified a new SUMO-interacting motif (SIM) in PIASy. The new SIM and the currently known SIM are both located at the C terminus of PIASy, and both are required for the full ligase activity of PIASy. Our results provide novel insights into the mechanism of PIASy-mediated SUMOylation. PIASy adds to the growing list of SUMO E3 ligases containing multiple SIMs that play important roles in the E3 ligase activity. |
| Databáze: | OpenAIRE |
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