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In Vitro Characterization of Sumoylation of HR Proteins
V. Altmannova, L. Krejci
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
206292/E/17/Z
Wellcome Trust - United Kingdom
- MeSH
- Escherichia coli genetics growth & development metabolism MeSH
- Homologous Recombination * MeSH
- Ubiquitin-Protein Ligase Complexes metabolism MeSH
- Small Ubiquitin-Related Modifier Proteins metabolism MeSH
- Escherichia coli Proteins metabolism MeSH
- Recombinant Proteins isolation & purification MeSH
- Sumoylation MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
In vitro analysis of posttranslational modifications such as sumoylation provides a great tool to not only identify the target proteins but also to characterize the specific effects of this modification on the protein features and uncover possible regulatory mechanism. In this chapter, we will describe the purification of yeast SUMO machinery proteins and their use to identify SUMO modification of target proteins in vitro. Furthermore, we will show several examples characterizing the effect of sumoylation on the biochemical activities of various proteins involved in homologous recombination (HR) that helped to better understand the regulatory role of this modification.
Department of Biology Masaryk University Brno Czech Republic
International Clinical Research Center St Anne's University Hospital Brno Czech Republic
National Center for Biomolecular Research Masaryk University Brno Czech Republic
References provided by Crossref.org
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