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dc.contributor.advisorPugh, David J.R.
dc.contributor.authorMlaza, Mihlali
dc.date.accessioned2018-08-06T12:29:23Z
dc.date.available2018-08-06T12:29:23Z
dc.date.issued2018
dc.identifier.urihttp://hdl.handle.net/11394/6200
dc.descriptionRetinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa protein shown to play a role in 3'- polyadenylation of mRNA transcripts, as well as to function as an E3 ligase catalysing ubiquitination of cancer-associated proteins. RBBP6 has been previously reported to localise to nuclear speckles, which are thought to play a role in mRNA splicing, presumably as a result of its RS domain, which is known to target mRNA splicing factors to nuclear speckles. However recent studies in our laboratory have shown that isoform 3 of RBBP6, consisting mainly of the DWNN domain, also localises to speckles in resting cells, but more strongly in cells subjected to various stresses, suggesting that the DWNN domain may be the speckle-targeting domain.
dc.description.abstractMagister Scientiae - MSc (Biotechnology)
dc.language.isoen
dc.publisherUniversity of the Western Cape
dc.subjectRBBP6
dc.subjectDWNN domain
dc.subjectProtein localisation
dc.subjectSite-directed mutagenesis
dc.subjectNuclear speckles
dc.titleInvestigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
dc.rights.holderUniversity of the Western Cape


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