Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/34454
Title: UNDERSTANDING THE MOLECULAR MECHANISM OF CENTRINS IN TRYPANOSOMA BRUCEI
Authors: ZHANG YU
Keywords: Trypanosoma brucei, TbCentrin2, TbCentrin4, Ca2+ binding, self assembly, binding partners
Issue Date: 1-Nov-2011
Source: ZHANG YU (2011-11-01). UNDERSTANDING THE MOLECULAR MECHANISM OF CENTRINS IN TRYPANOSOMA BRUCEI. ScholarBank@NUS Repository.
Abstract: <i>Trypanosoma brucei</i> is the causative agent of sleeping sickness in humans and Nagana in livestock. In addition to its medical and economic importance, this unicellular eukaryote is a powerful model to address fundamental questions on organelle biogenesis and positioning during the cell cycle. Both TbCentrin2 and TbCentrin4, belonging to the calmodulin superfamily, have been demonstrated to be essential for <i>T. brucei</i>. In addition to the basal bodies, both centrins mark a bi-lobed structure, which is important for coordinated organelle segregation during <i>T. brucei</i> cell division. Despite their sequence similarity and cellular colocalization, previous RNAi experiments revealed their distinct functions in organelle duplication and cell cycle progression. This thesis further investigated the molecular mechanisms of TbCentrin2 and TbCentrin4. Biophysical studies confirmed the Ca<sup>2+</sup> binding ability of both TbCentrins. Additionally, Ca<sup>2+</sup>-dependent self-assembly was observed with TbCentrin2 but not TbCentrin4, which may partially explain the functional difference of these two TbCentrins. Efforts were also made to identify binding partners of TbCentrin2 and TbCentrin4 in <i>T. brucei</i>. Putative candidates were evaluated for their cellular localization and molecular function. These studies provided insight into the functional diversity of centrins as well as useful reagents for further investigation of centrin mechanisms.
URI: http://scholarbank.nus.edu.sg/handle/10635/34454
Appears in Collections:Master's Theses (Open)

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