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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1

Muleya, Victor January 2010 (has links)
<p>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 directed yeast 2-hybrid assay, co-immunoprecipitation and NMR chemical shift perturbation analysis. Our results suggest that the entire 62 amino acid region at the C-terminal domain of YB-1 may be involved in the interaction with RBBP6. Using chemical shift perturbation analysis, this study provides an indication of where YB-1 binds to the RING finger. This represents the first step towards the design of therapeutics aimed at modulating the interaction between RBBP6 and YB-1 as a means of targeting the oncogenic effects of YB-1. In order to identify E2 enzymes involved in the ubiquitination of YB-1, we examined the efficiencies of selected E2s in an in vitro ubiquitination assay. UbcH5c and UbcH7 were both found to catalyse the ubiquitination of YB-1 in conjuction with RBBP6, whereas Ubc13 was not. Finally, we show using NMR that two single-point mutations of the RING finger-like domain are sufficient to abolish homodimerisation of the domain. These will be used in future studies to investigate the requirement for homodimerisation on the ubiquitination activity of RBBP6.</p>
2

Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1

Muleya, Victor January 2010 (has links)
<p>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 directed yeast 2-hybrid assay, co-immunoprecipitation and NMR chemical shift perturbation analysis. Our results suggest that the entire 62 amino acid region at the C-terminal domain of YB-1 may be involved in the interaction with RBBP6. Using chemical shift perturbation analysis, this study provides an indication of where YB-1 binds to the RING finger. This represents the first step towards the design of therapeutics aimed at modulating the interaction between RBBP6 and YB-1 as a means of targeting the oncogenic effects of YB-1. In order to identify E2 enzymes involved in the ubiquitination of YB-1, we examined the efficiencies of selected E2s in an in vitro ubiquitination assay. UbcH5c and UbcH7 were both found to catalyse the ubiquitination of YB-1 in conjuction with RBBP6, whereas Ubc13 was not. Finally, we show using NMR that two single-point mutations of the RING finger-like domain are sufficient to abolish homodimerisation of the domain. These will be used in future studies to investigate the requirement for homodimerisation on the ubiquitination activity of RBBP6.</p>
3

Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-1

Muleya, Victor January 2010 (has links)
Magister Scientiae - MSc / 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 directed yeast 2-hybrid assay, co-immunoprecipitation and NMR chemical shift perturbation analysis. Our results suggest that the entire 62 amino acid region at the C-terminal domain of YB-1 may be involved in the interaction with RBBP6. Using chemical shift perturbation analysis, this study provides an indication of where YB-1 binds to the RING finger. This represents the first step towards the design of therapeutics aimed at modulating the interaction between RBBP6 and YB-1 as a means of targeting the oncogenic effects of YB-1. In order to identify E2 enzymes involved in the ubiquitination of YB-1, we examined the efficiencies of selected E2s in an in vitro ubiquitination assay. UbcH5c and UbcH7 were both found to catalyse the ubiquitination of YB-1 in conjuction with RBBP6, whereas Ubc13 was not. Finally, we show using NMR that two single-point mutations of the RING finger-like domain are sufficient to abolish homodimerisation of the domain. These will be used in future studies to investigate the requirement for homodimerisation on the ubiquitination activity of RBBP6. / South Africa
4

Structural characterisation of the interaction between RBBP6 and the multifunctional protein YB-l

Muleya, Victor January 2010 (has links)
>Magister Scientiae - MSc / Retinoblastoma binding protein 6 (RBBP6) is a 250 kDa RING finger-containing protein whose function is known to be mediated through interaction with other proteins. RBBP6 plays a role in the regulation of the tumour suppressor protein p53 and is also thought to be involved in mRNA splicing although its role has yet to be characterised. A recent study utilising a yeast 2-hybrid screen identified the cancer-associated protein known as YB-l as an interacting partner of RBBP6, and showed that RBBP6 ubiquitinates YB-I, leading to its degradation in the proteasome.Human Y-box binding protein 1 (YB-I) is member of the cold-shock domain family of proteins, which regulates a number of growth related genes through both transcriptional and translational mechanisms. YB-l is a cell-survival factor whose expression is increased in proliferating normal and cancer cells. It also protects cells against p53-mediated apoptosis by repressing the p53- promoter and down-regulating endogenous p53. The interaction between RBBP6 and YB-l involves the RING finger-like domain ofRBBP6 and the C-terminal62 amino acids ofYB-l. As a means of further localising the interaction, truncated fragments derived from the C-terminal region of YB-I, were tested for their interaction with the RING finger domain of RBBP6 using three different assays: a directed yeast 2-hybrid assay, co-immunoprecipitation and NMR chemical shift perturbation analysis. Our results suggest that the entire 62 amino acid region at the C-terminal domain ofYB-l may be involved in the interaction with RBBP6. Using chemical shift perturbation analysis, this study provides an indication of where YB-l binds to the RING fmger. This represents the first step towards the design of therapeutics aimed at modulating the interaction between RBBP6 and YB-l as a means of targeting the oncogenic effects ofYB-l. In order to identify E2 enzymes involved in the ubiquitination of YB-I, we examined the efficiencies of selected E2s in an in vitro ubiquitination assay. UbcH5c and UbcH7 were both found to catalyse the ubiquitination of YB-l in conjuction with RBBP6, whereas Ubc 13 was not. Finally, we show using NMR that two single-point mutations of the RING finger-like domain are sufficient to abolish homodimerisation of the domain. These will be used in future studies to investigate the requirement for homodimerisation on the ubiquitination activity of RBBP6. www.etd.
5

Localization and dimerization of the ABC half transporter rAbcb6 as compared to rAbcb7 / Lokalisation und Dimerisation des Ratten-ABC-Halbtransporters, rAbcb6 im Vergleich zu rAbcb7

Jakimenko, Ana 06 July 2006 (has links)
No description available.

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