Browsing by Author "Pugh, David J.R."
Now showing items 1-15 of 15
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An investigation of the zinc binding characteristics of the RING finger domain from the human RBBP6 protein using heteronuclear NMR spectroscopy.
Mulaudzi, Takalani (University of the Western Cape, 2007)Retinoblastoma binding prot ein 6 (RBBP6) is a 250 kDa human splicing-associated protein that is also known to interact with tumour suppresso r proteins p53 and pRb and to mediate ubiquitination of p53 via its ... -
Characterisation of N-terminal fragments of Retinoblastoma Binding Protein 6 for structural analysis
Maumela, Matodzi Portia (University of the Western Cape, 2016)Retinoblastoma Binding Protein 6 (RBBP6) is a 200 kDa RING finger-containing protein that plays a role in 3'-end poly-adenylation of mRNA transcripts as well as acting as an E3 ubiquitin ligase against a number of proteins ... -
Expression and purification of the novel protein domain DWNN
Lutya, Portia Thandokazi (University of the Western Cape, 2002)Proteins play an important role in cells, as the morphology, function and activities of the cell depend on the proteins they express. The key to understanding how different proteins function lies in an understanding of the ... -
In vitro investigation of putative interactions between the RING finger domain of Retinoblastoma Binding Protein 6 (RBBP6) and various substrates
Witbooi, Christopher Jerome (University of the Western Cape, 2015)Retinoblastoma Binding Protein 6 (RBBP6) is a RING finger-containing protein which plays a critical role in the 3'-end processing of mRNA transcripts. It is a constituent of the human pre-mRNA processing complex but also ... -
In vitro investigation of the ubiquitination and degradation of p53 by Murine Double Minute 2 (MDM2) and Retinoblastoma Binding Protein 6 (RBBP6)
Jooste, Lauren Sarah (University of the Western Cape, 2015)P53 is one of the most important tumour suppressor proteins in the body which protects the cell against the tumourigenic effects of DNA damage by initiating processes such as apoptosis, senescence and cell cycle arrest. ... -
Investigation of protein-metal ion and protein-protein interactions using mass spectrometry and nuclear magnetic spectroscopy
Hassem, Faqeer A. (University of Western Cape, 2014)Protein-protein interaction networks provide a global picture of cellular function and biological processes. Some proteins act as hub proteins, highly connected to others, whereas some others have few interactions. The ... -
Investigation of the interaction of ceramide and acyl-coenzyme A with the mitochondrial associated protein, endozepine, using heteronuclear NMR
Onyemata, Ezenwa James (University of the Western Cape, 2005)Endozepine is an alternative name for the testis-specific isoform of the acyl-CoA binding protein (t-ACBP). Acyl-CoA binding proteins form a highly conserved family of proteins, which bind long chain fatty acid esters with ... -
Investigation of the interactions of retinoblastoma binding protein-6 with transcription factors p53 and Y-Box Binding Protein-1
Faro, Andrew (2011)Retinoblastoma Binding Protein 6 (RBBP6) is a 250 kDa multi-domain protein that has been implicated in diverse cellular processes including apoptosis, mRNA processing and cell cycle regulation. Many of these functions are ... -
Investigation of the role of the ubiquitin-like DWNN domain in targeting Retinoblastoma Binding Protein 6 to nuclear speckles
Mlaza, Mihlali (University of the Western Cape, 2018)Magister Scientiae - MSc (Biotechnology) -
Recombinant expression and full backbone assignment of the human DWNN using heteronuclear NMR
Faro, Andrew (University of the Western Cape, 2005)The cellular levels of a number of proteins have been found to be regulated by the ubiquitin-proteasome pathway. In this pathway, proteins are covalently tagged (“ubiquitinated”) by ubiquitin, which acts as a signal for ... -
Recombinant expression of the pRb- and p53-interacting domains from the human RBBP6 protein for in vitro binding studies
Ndabambi, Nonkululeko (University of the Western Cape, 2004)This thesis describes the cloning and recombinant expression of domains from the human RBBP6 protein for future in vitro binding studies with pRb and p53. RBBP6 is a splicing-associated protein that is known to interact ... -
Solution structure of the RING finger domain from the human splicing-associated protein RBBP6 using heteronuclear Nuclear Magnetic Resonance (NMR) spectroscopy
Pugh, David J.R. (2009)Retinoblastoma-binding protein 6 (RBBP6) is a multi-domain human protein known to play a role in mRNA splicing, cell cycle control and apoptosis. The protein interacts with tumour suppressor proteins p53 and pRb and recent ... -
Structural and functional studies of XvPrx2, a type II peroxiredoxin protein from the resurrection plant xerophyta viscosa
Onyemata, Ezenwa James (University of the Western Cape, 2012)XvPrx2 is a 1-Cys-containing member of the Prx5 subfamily of peroxiredoxins isolated from the resurrection plant Xerophyta viscosa. It is reported to be up-regulated during periods of desiccation and to protect nucleic ... -
Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1
Muleya, Victor (University of the Western Cape, 2010)As a means of further localising the interaction, truncated fragments derived from the C-terminal region of YB-1, were tested for their interaction with the RING finger domain of RBBP6 using three different assays: a ... -
A yeast 2-hybrid screen to identify and characterize interaction partners of the cancer associated protein retinoblastoma binding protein 6
Chibi, Moredreck (2009)Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa protein that is implicated in mRNA processing and ubiquitination functions and has been shown to be highly up-regulated in a number of cancers. In humans and mice,RBBP6 ...