ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin
| Autor: | Oxana A. Malakhova, Vladimir Papov, Keun Il Kim, Weiguo Zou, Chinh T. Dao, Dong-Er Zhang, Jun Li |
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| Rok vydání: | 2005 |
| Předmět: |
Molecular Sequence Data
Biophysics Thioester Biochemistry Mass Spectrometry Ubiquitin Humans Amino Acid Sequence Molecular Biology Peptide sequence Ubiquitins chemistry.chemical_classification biology Mutagenesis Esters Cell Biology ISG15 Ubiquitin ligase chemistry Covalent bond Ubiquitin-Conjugating Enzymes biology.protein Cytokines Function (biology) |
| Zdroj: | Biochemical and biophysical research communications. 336(1) |
| ISSN: | 0006-291X |
| Popis: | ISG15 was the first ubiquitin-like modifier to be identified. However, the function of ISG15 modification has been an enigma for many years. At present, no data are available about the function of ISGylation for any target. In this paper, we report the identification of Ubc13, which forms a unique ubiquitin-conjugating enzyme (Ubc) complex with ubiquitin enzyme variant Mms2 and generates atypical Lys63-linked ubiquitin conjugates, as one of the targets of ISG15 modification. Furthermore, we identify Lys92 as the only ISG15 modification site in Ubc13, which is the first report about the ISG15 modification site. Using the "covalent affinity" purification assay, we found that unmodified Ubc13 can bind to the ubiquitin-agarose, whereas ISGylated Ubc13 cannot. This result indicates that ISGylation of Ubc13 disrupts its ability to form thioester bond with ubiquitin. |
| Databáze: | OpenAIRE |
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