Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/19015
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dc.contributor.authorThaker, Youg Rajen
dc.date.accessioned2009-09-09T07:58:19Zen
dc.date.available2009-09-09T07:58:19Zen
dc.date.copyright2009en
dc.date.issued2009en
dc.identifier.citationThaker, Y. R. (2009). Caspase interaction of anti-apoptotic Livin as well as the vacuolar ATPase (V-ATPase) and structural insights into the subunit d and a of the yeast V-ATPase. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.identifier.urihttps://hdl.handle.net/10356/19015en
dc.description.abstractApoptosis is a critical process to remove the non-functional and redundant cells regulated by pro- and anti-apoptotic factors. Perturbation of balance between pro- and anti-apoptotic components is the leading cause of several physiopathological conditions such as neurodegenerative and cancer malignancies. Here, the pro-apoptotic cellular protein, ARTS as well as an anti-apoptotic protein, Livin, a family member of inhibitor of apoptosis have been studied. Results showed that ARTS is not the target of Livin E3 ligase activity in apoptotic cells co-expressing ARTS and Livin. In turn, Livin was found to undergo cleavage in ARTS promoted apoptosis which was independent of its self-ubiquitination activity, normally observed in healthy cells. The exhaustion of Livin during ARTS-promoted apoptosis could partially be suppressed by the caspase inhibitors, implying a possible role of caspases concomitant with high active caspase 7 levels found in ARTS-promoted staurosporine-induced apoptosis. Not only Livin, caspase do cleave several important cellular components during apoptosis and here, I have identified subunit d of V-ATPase as a new target of caspase 3. V ATPases do play critical role in health and disease by maintaining proper acid/base balance pH. Additionally, homogenous protein preparation of yeast subunit d protein was used to determine its first low resolution shape by small angle X-ray spectroscopy (SAXS), revealing two distinct domains of 6.5 nm and 3.5 nm widths forming a “boxing glove” shape. Using previously solved low resolution structure of VO domain as a template, subunit d could be assigned inside the VO, allowing its clear localization on the top of VO domain of V-ATPase. Moreover, biochemical approaches of fluorophore labeling, tryptic digestion and MALDI-TOF analysis led to the identification of a cysteine bridge between Cys36 and Cys329.en
dc.format.extent190 p.en
dc.language.isoenen
dc.subjectDRNTU::Science::Biological sciences::Human anatomy and physiologyen
dc.titleCaspase interaction of anti-apoptotic Livin as well as the Vacuolar ATPase (V-ATPase) and structural insights into the subunit d and a of the yeast V-ATPaseen
dc.typeThesisen
dc.contributor.supervisorGerhard Gruberen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
dc.identifier.doi10.32657/10356/19015en
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