The Small Ubiquitin-like Modifier-1 (SUMO-1) Consensus Sequence Mediates Ubc9 Binding and Is Essential for SUMO-1 Modification
| Autor: | Michael J. Matunis, Min Wang, Deborah A. Sampson |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Protein sumoylation
DNA Complementary Reticulocytes SUMO-1 Protein Recombinant Fusion Proteins genetic processes SUMO enzymes SUMO binding macromolecular substances Ubiquitin-conjugating enzyme Biology environment and public health Biochemistry Ligases Small Ubiquitin-Related Modifier Proteins Consensus Sequence Animals Humans Amino Acid Sequence Ubiquitins Molecular Biology Peptide sequence Conserved Sequence Sequence Deletion Binding Sites Sequence Homology Amino Acid Cell Biology Sumoylation Pathway Recombinant Proteins enzymes and coenzymes (carbohydrates) Liver Protein Biosynthesis Ubiquitin-Conjugating Enzymes health occupations Rabbits Sequence Alignment Plasmids Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 276:21664-21669 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m100006200 |
| Popis: | SUMO-1 is an ubiquitin-related protein that is covalently conjugated to a diverse assortment of proteins. The consequences of SUMO-1 modification include the regulation of protein-protein interactions, protein-DNA interactions, and protein subcellular localization. At present, very little is understood about the specific mechanisms that govern the recognition of proteins as substrates for SUMO-1 modification. However, many of the proteins that are modified by SUMO-1 interact directly with the SUMO-1 conjugating enzyme, Ubc9. These interactions suggest that Ubc9 binding may play an important role in substrate recognition as well as in substrate modification. The SUMO-1 consensus sequence (SUMO-1-CS) is a motif of conserved residues surrounding the modified lysine residue of most SUMO-1 substrates. This motif conforms to the sequence "PsiKXE," where Psi is a large hydrophobic residue, K is the lysine to which SUMO-1 is conjugated, X is any amino acid, and E is glutamic acid. In this study, we demonstrate that the SUMO-1-CS is a major determinant of Ubc9 binding and SUMO-1 modification. Mutating residues in the SUMO-1-CS abolishes both Ubc9 binding and substrate modification. These findings have important implications for how SUMO-1 substrates are recognized and for how SUMO-1 is ultimately transferred to specific lysine residues on these substrates. |
| Databáze: | OpenAIRE |
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