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dc.contributor.advisorPugh, David
dc.contributor.authorChen, Po-An
dc.date.accessioned2021-02-25T09:57:27Z
dc.date.issued2019
dc.identifier.urihttp://hdl.handle.net/11394/7893
dc.description>Magister Scientiae - MScen_US
dc.description.abstractRetinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa multi-domain protein that has been shown to play a role in mRNA processing, cell cycle arrest and apoptosis. RBBP6 interacts with tumour suppressor proteins such as p53 and pRb and has been shown cooperate with Murine Double Minute 2 (MDM2) protein in catalyzing ubiquitination and suppression of p53. Unpublished data from our laboratory has suggested that RBBP6 and MDM2 interact with each other through their RING finger domains. RBBP6 has also been shown to have its own E3 ubiquitin ligase activity, catalyzing ubiquitination of Y-Box Binding Protein 1 (YB-1) in vitro and in vivo. YB- 1 is a multifunctional oncogenic protein that is generally associated with poor prognosis in cancer, tumourigenesis, metastasis and chemotherapeutic resistance. Unpublished data from our laboratory shows that RBBP6 catalyzes poly-ubiquitination of YB-1, using Ubiquitin-conjugating enzyme H1 (UbcH1) as E2 ubiquitin conjugating enzyme.en_US
dc.language.isoenen_US
dc.publisherUniversity of Western Capeen_US
dc.subjectRetinoblastoma binding protein 6en_US
dc.subjectChemotherapeutic resistanceen_US
dc.subjectNuclear magnetic resonance (NMR) spectroscopyen_US
dc.subjectInteractionen_US
dc.titleInvestigation of protein-protein interactions involving retinoblastoma binding protein 6 using immunoprecipitation and nuclear magnetic resonance spectroscopyen_US
dc.rights.holderUniversity of Western Capeen_US
dc.description.embargo2022-02-25


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