Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system

Mikako Hirohama, Arnout R.D. Voet, Takeaki Ozawa, Hisato Saitoh, Yoichi Nakao, Kam Y.J. Zhang, Akihiro Ito, Minoru Yoshida

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)92-94
Number of pages3
JournalAnalytical Biochemistry
Volume448
Issue number1
DOIs
Publication statusPublished - 2014 Mar 1

Keywords

  • Assay
  • Protein-protein interactions
  • SIM
  • SUMOylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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