Protein-Protein interaction assay utilizing SUMOylation
Referenznummer TO 15-00038
The Challenge
Today various methods exist for identifying and verifying protein interactions in cells (e.g. Two-Hybrid, co-precipitation, pull-down). A drawback of said systems is the detection of falls positive interaction due to wrong activation of reporter genes which may be due to the fact that human or other mammal proteins are analyzed in a yeast or E. coli system. In addition, the protein interaction may occur in an environment which does not equal the natural situation. Artificial protein interaction may take place in the artificial cell extract which does not display the natural situation present in a cellular environment.
Therefore, there is still a demand for new methods and systems allowing in vivo screening for and/or detection of molecular interactions.
In addition, there is an ongoing demand for methods allowing screening for and/or detection of SUMOylation of target molecules.
Technology
Protein SUMOylation is a reversible conjugation process with strong similarity to ubiquitination and is involved in the regulation of several proteins. The present technology relates to vector based methods for determining SUMOylation patterns which can be utilized to identify protein-protein interactions and building of multiprotein complexes. Assays can be conducted in mammalian cell lines as well as cell free systems.
Commercial Opportunity
In-licensing of an innovative technology suitable for the development of kits for
- in vivo verification and identification of protein-protein
interactions
- detailed studies of protein SUMOylation
Research tool for the analysis of protein interactions in mammalian cells with reduced artificial binding allowing identification of binding partners in their natural environment.
Developmental Status
Research Tool
Patent Situation
European patent application EP 08013924.9 is pending, a PCT application is in preparation.
Further Reading
Srivastav et al. (2011) Monitoring protein-protein-interactions in mammalian cells by Trans-SUMOylation. Biochemical Journal Immediate Publication. Published on 15 Jun 2011 as manuscript BJ20110035.
Zimnik et al. (2009) Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation. Nucleic Acids Res. Mar;37(4):e30. Epub 2009 Jan 27.
Jakobs et al. (2007) Ubc9 fusion–directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation. Nature Methods - 4, 245 – 250.
