Interaction properties of hnRNP-U family proteins AND SIM:SUMO interaction of the deSUMOylation enzyme SENP7 and the SIMs role in protein functionality

Pratt, Kenny (2012). Interaction properties of hnRNP-U family proteins AND SIM:SUMO interaction of the deSUMOylation enzyme SENP7 and the SIMs role in protein functionality. University of Birmingham. M.Res.

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Abstract

Project 1: HnRNPs have recently been shown to have roles within the DNA damage response (DDR) through direct protein-protein interactions. Within this study, interactions between the hnRNP-U-like proteins (1 and 2) and p53, CtIP and BLM were confirmed both in vitro and in vivo and mapped to particular regions. A novel interaction of the hnRNP-ULs with PARP was also identified. The protein-protein interactions of the hnRNP-ULs shown within this study and in various other studies reveal a link between hnRNP-U-like proteins and DNA damage response proteins, and verify the extensive associations and potential roles of hnRNP-U-like proteins within the DDR.

Project 2: The post-translational protein modification, SUMOylation, has been identified as playing a key role in the DNA damage response (DDR). Previous work in our laboratory had shown the deSUMOylation enzyme SENP7 to be recruited to sites of DNA repair and essential for execution of homologous recombination (HR). To cleave poly-SUMO-2/3 chains as SENP7 is known to do, it was expected that the protein would employ SUMO-interaction motifs (SIMs) to bind SUMO. This project showed the 7 identified potential SIMs of SENP7 were of critical importance both for interaction with SUMO-2-modified proteins and the functionality of the protein within its role in homologous recombination (HR).

Type of Work:

Thesis (Masters by Research > M.Res.)

Award Type:

Masters by Research > M.Res.

Supervisor(s):