SUMO has diverse roles in cellular physiology that in most cases are mediated by its ability to interact non-covalently with hydrophobic patches of low sequence complexity known as SUMO Interaction Motifs (SIMs). Extensive proteomic analysis has documented the co-ordinate SUMO modification of many components of large nucleoprotein complexes. An emerging mode of action of SUMO is that multiple members of large protein complexes, rather than single proteins, are targeted for modification by the limited number of SUMO E3 ligases. Although the modification of components of the complexes may be sub-stoichiometric this still allows them to interact non-covalently with the more abundant SIM sequences. This serves to increase the stability of the complex such that it attains or retains biological activity. In this situation SUMO modification is acting as a relatively unspecific biological glue.
The aim of the project is to determine the molecular basis for the recognition of the nucleoprotein complexes and the SUMO modification of their protein components.
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