Introduction: This project aims to investigate the role of retinoblastoma binding protein 7 (RBBP7) in maintaining genomic stability (a universal cancer hallmark) through an interaction with the components of a previously undescribed chromatin-remodelling complex named as the Histone Ubiquitin Remodelling Complex (HURC). Additionally, the project will determine the role of the HURC complex in DNA double strand break (DNA DSB) repair and investigate the role RBBP7 plays in lung and breast cancer development, progression and resistance.
We hypothesise that RBBP7 functions as part of a novel Histone Ubiquitin Remodelling Complex (HURC) that is critical for genomic stability.
Methods: Liquid chromatography mass spectrometry (LC-MS) using a method of Q exactive HF was used to determine which components of the HURC complex interact with RBBP7. Confirmation of protein interactions were performed by co-immunoprecipitations.
Results: LC-MS results have shown that RBBP7 interacts with several proteins that are part of the copper metabolism gene MURR1 (COMMD) family. Co-immunoprecipitations have confirmed that RBBP7 interacts with some of the HURC components.
Conclusion: LC-MS has opened a range of unexplored possible interactions that can be further confirmed through co-immunoprecipitations and that might be involved in genomic stability and other relevant molecular pathways. RBBP7 interacts with some of the HURC components and other DNA repair proteins suggesting that it may play a role in DNA repair.