Purification and identification of endogenous polySUMO conjugates
| Autor: | Ronald T. Hay, Amit K. Garg, Anna Plechanovová, Roland Bruderer, Ivan Matic, Michael H. Tatham |
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| Rok vydání: | 2011 |
| Předmět: |
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Proteome Molecular Sequence Data SUMO protein Plasma protein binding Biology Biochemistry Affinity chromatography Stress Physiological Genetics Humans Protein Interaction Domains and Motifs Amino Acid Sequence Nuclear protein Molecular Biology Peptide sequence Gene Transcription factor Scientific Reports Nuclear Proteins Sumoylation HeLa Cells Protein Binding Subcellular Fractions Transcription Factors |
| Zdroj: | EMBO Rep |
| ISSN: | 1469-3178 1469-221X |
| Popis: | The small ubiquitin-like modifier (SUMO) can undergo self-modification to form polymeric chains that have been implicated in cellular processes such as meiosis, genome maintenance and stress response. Investigations into the biological role of polymeric chains have been hampered by the absence of a protocol for the purification of proteins linked to SUMO chains. In this paper, we describe a rapid affinity purification procedure for the isolation of endogenous polySUMO-modified species that generates highly purified material suitable for individual protein studies and proteomic analysis. We use this approach to identify more than 300 putative polySUMO conjugates from cultured eukaryotic cells. |
| Databáze: | OpenAIRE |
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