Publication details
Study of Rad52 SUMOylation
| Authors | |
|---|---|
| Year of publication | 2008 |
| Type | R&D Presentation |
| MU Faculty or unit | |
| Citation | ALTMANNOVÁ, Veronika and Lumír KREJČÍ. Study of Rad52 SUMOylation. 2008. |
| Description | Rad52 is a DNA-binding protein which plays a key role in a maintenance of genomic integrity and is essential for the error-free repair of DNA double-strand breaks (DSBs) by homologous recombination (HR). It mediates the exchange of the recombination factor RPA associated to single-stranded DNA (ssDNA) by Rad51, resulting in the assembly of the presynaptic filament. Recently, it has been reported that upon DNA damage Rad52 is modified by the small ubiquitin-like modifier (SUMO) protein which shelters Rad52 against proteosomal degradation. As the major SUMOylation sites of Rad52, three lysines (K43, K44, K253) have been identified. The effect of Rad52 DNA binding and interaction with its partners was tested to clarify the regulatory mechanism of Rad52 SUMOylation. |
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