期刊
ANALYTICAL BIOCHEMISTRY
卷 448, 期 -, 页码 92-94出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2013.12.009
关键词
Assay; SIM; SUMOylation; Protein-protein interactions
资金
- Chemical Genomics Research Project, RIKEN Center for Sustainable Resource Science, RIKEN Initiative Research Unit program
- JSPS
- CREST
- Japan Science and Technology Corporation
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Grants-in-Aid for Scientific Research [12F02509, 23616004, 23510288, 26220805] Funding Source: KAKEN
SUMOylation is a posttranslational process that attaches a small ubiquitin-like modifier (SUMO) to its target proteins covalently. SUMOylation controls multiple cellular processes through the recognition of SUMO by a SUMO-interacting motif (SIM). In this study, we developed assay systems for detecting noncovalent interactions between SUMO and SIM in cells using split-luciferase complementation. We applied a version of this assay to the detection of in vitro SUMO-SIM interactions using a bacterial expression system. These novel assays enable screening of inhibitors of SUMO-dependent protein-protein interactions, either in vivo or in vitro, in a high-throughput manner. (C) 2013 Elsevier Inc. All rights reserved.
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