Covalent Modification of p73α by SUMO-1
| Autor: | Xavier Dumont, Mourad Kaghad, Adrian Minty, Daniel Caput |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
SUMO-1 Protein genetic processes Lysine SUMO protein SUMO binding macromolecular substances Cell Biology Plasma protein binding Biology environment and public health Biochemistry Amino acid enzymes and coenzymes (carbohydrates) chemistry health occupations Thymine-DNA glycosylase Molecular Biology Peptide sequence |
| Zdroj: | Journal of Biological Chemistry. 275:36316-36323 |
| ISSN: | 0021-9258 |
| Popis: | Two-hybrid screening in yeast with p73alpha isolated SUMO-1 (small ubiquitin-like modifier 1), the enzyme responsible for its conjugation, Ubc-9, and a number of novel SUMO-1-interacting proteins, including thymine DNA glycosylase, PM-Scl75, PIASx, PKY, and CHD3/ZFH. A subset of these proteins contain a common motif, hhXSXS/Taaa, where h is a hydrophobic amino acid and a is an acidic amino acid, that is shown to interact with SUMO-1 in the two-hybrid system. We show here that p73alpha, but not p73beta, can be covalently modified by SUMO-1. The major SUMO-1-modified residue in p73alpha is the C-terminal lysine (Lys(627)). The sequence surrounding this lysine conforms to a consensus SUMO-1 modification site b(X)XXhKXE, where b is a basic amino acid. SUMO-1-modified p73 is more rapidly degraded by the proteasome than unmodified p73, although SUMO-1 modification is not required for p73 degradation. SUMO-1 modification does not affect the transcriptional activity of p73alpha on an RGC-luciferase reporter gene in SK-N-AS cells. Instead, SUMO-1 modification may alter the subcellular localization of p73, because SUMO-1-modified p73 is preferentially found in detergent-insoluble fractions. Alternatively, it may modulate the interaction of p73 with other proteins that are substrates for SUMO-1 modification or which interact with SUMO-1, such as those identified here. |
| Databáze: | OpenAIRE |
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