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Purification and identification of endogenous polySUMO conjugates
Roland Bruderer1, Michael H Tatham, Anna Plechanovova
1Wellcome Trust Centre for Gene Regulation and Expression, Dow Street, Dundee DD1 5EH, UK.
EMBO Reports
|January 22, 2011
Summary
Researchers developed a new method to purify small ubiquitin-like modifier (SUMO) chains, enabling the study of their cellular roles. This technique identified over 300 SUMO-modified proteins in eukaryotic cells.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Polymeric chains of small ubiquitin-like modifier (SUMO) are involved in crucial cellular processes like meiosis, genome maintenance, and stress response.
- Studying the biological functions of SUMO chains has been challenging due to the lack of effective purification protocols for SUMO-chain-modified proteins.
Purpose of the Study:
- To develop a rapid and efficient affinity purification procedure for isolating endogenous polySUMO-modified species.
- To enable detailed studies of individual proteins and proteomic analysis of polySUMO conjugates.
Main Methods:
- A novel rapid affinity purification protocol was established.
- The protocol was applied to isolate endogenous polySUMO-modified proteins from cultured eukaryotic cells.
Main Results:
- The developed procedure yields highly purified polySUMO-modified species.
- Over 300 putative polySUMO conjugates were identified in eukaryotic cells using this method.
Conclusions:
- The new purification technique overcomes previous limitations in studying SUMO chain biology.
- This advancement facilitates comprehensive proteomic analysis and investigation into the roles of polySUMOylation in cellular functions.
