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Analysis of modification and proteolytic targeting by the ubiquitin-like modifier FAT10.
Aichem, Annette; Boehm, Annika N; Catone, Nicola; Schmidtke, Gunter; Groettrup, Marcus.
Afiliación
  • Aichem A; Biotechnology Institute Thurgau at the University of Konstanz, Kreuzlingen, Switzerland; Division of Immunology, Department of Biology, University of Konstanz, Konstanz, Germany.
  • Boehm AN; Biotechnology Institute Thurgau at the University of Konstanz, Kreuzlingen, Switzerland; Division of Immunology, Department of Biology, University of Konstanz, Konstanz, Germany.
  • Catone N; Biotechnology Institute Thurgau at the University of Konstanz, Kreuzlingen, Switzerland.
  • Schmidtke G; Division of Immunology, Department of Biology, University of Konstanz, Konstanz, Germany.
  • Groettrup M; Biotechnology Institute Thurgau at the University of Konstanz, Kreuzlingen, Switzerland; Division of Immunology, Department of Biology, University of Konstanz, Konstanz, Germany. Electronic address: marcus.groettrup@uni-konstanz.de.
Methods Enzymol ; 618: 229-256, 2019.
Article en En | MEDLINE | ID: mdl-30850054
The ubiquitin-like modifier FAT10 (also called ubiquitin D (UBD)) interacts noncovalently with a substantial number of proteins and also gets covalently conjugated to many substrate proteins, leading to their degradation by the 26S proteasome. FAT10 comprises two loosely folded ubiquitin-like domains that are connected by a flexible linker, and this unusual structure makes it highly prone to aggregation. Here, we report methods to purify high amounts of soluble recombinant FAT10 for various uses, such as in vitro FAT10ylation assays. In addition, we describe how to generate and handle overexpressed as well as endogenous FAT10 in cellulo for use in immunoprecipitations, Western blot analyses, and FAT10 degradation studies.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitinas Límite: Humans Idioma: En Revista: Methods Enzymol Año: 2019 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitinas Límite: Humans Idioma: En Revista: Methods Enzymol Año: 2019 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos