Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis
| Autor: | David C.H. Yang, Earl R. Stadtman, Tianwei Li, Evgenij Evdokimov, Ephrem Tekle, Rong-Fong Shen, Tao Wang, P B Chock, Chien-Chung Chao |
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| Rok vydání: | 2004 |
| Předmět: |
Proteomics
Immunoprecipitation genetic processes SUMO protein SUMO enzymes macromolecular substances Biology In Vitro Techniques Heterogeneous ribonucleoprotein particle environment and public health Heterogeneous-Nuclear Ribonucleoproteins Cell Line Small Ubiquitin-Related Modifier Proteins Humans Amino Acid Sequence Nuclear pore Zinc finger Multidisciplinary Zinc Fingers Biological Sciences Recombinant Proteins Nuclear Pore Complex Proteins enzymes and coenzymes (carbohydrates) Biochemistry RNA splicing health occupations Protein Processing Post-Translational |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 101(23) |
| ISSN: | 0027-8424 |
| Popis: | SUMO, a small ubiquitin-related modifier, is known to covalently attach to a number of nuclear regulatory proteins such as p53, IκB, promyelocytic leukemia protein and c-Jun. The sumoylation reaction is catalyzed by the SUMO protease, which exposes the C-terminal active glycine residue of the nascent SUMO, the heterodimeric SUMO activating enzyme, the SUMO conjugating enzyme, Ubc9, and SUMO protein ligases, in a manner similar to ubiquitinylation. Identification of SUMO-regulated proteins is hampered by the fact that many sumoylated proteins are present at a level below normal detection limit. This limitation was overcome by either in vivo overexpression of Myc-SUMO or in vitro sumoylation with excess biotin–SUMO and Ubc9. Sumoylated proteins so obtained were affinity purified or isolated by immunoprecipitation. The isolated sumoylated proteins were identified by sequence analysis using mass spectrometric methods. Results reveal that several heterogeneous nuclear ribonucleoproteins (hnRNPs), zinc finger proteins, and nuclear pore complex proteins were sumoylated. The sumoylation of hnRNP A1, hnRNP F, and hnRNP K were confirmed in vivo by coimmunoprecipitation. In view of the facts that hnRNPs have been implicated in RNA splicing, transport, stability, and translation, our findings suggest that sumoylation could play an important role in regulating mRNA metabolism. |
| Databáze: | OpenAIRE |
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