Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/43569
Title: Biochemical characterization of the bi-lobe complex in Trypanosoma brucei
Authors: LADAN GHEIRATMAND
Keywords: Trypanosoma brucei, bilobe, organelle inheritance, proteomics, Spef1, TbLRRP1
Issue Date: 18-Apr-2013
Source: LADAN GHEIRATMAND (2013-04-18). Biochemical characterization of the bi-lobe complex in Trypanosoma brucei. ScholarBank@NUS Repository.
Abstract: Trypanosoma brucei, a unicellular parasite, contains several single-copied organelles that duplicate and segregate in a highly co-ordinated fashion during the cell cycle. In the procyclic stage of the parasite, a bi-lobed structure is found adjacent to the single ER exit site and Golgi apparatus near the flagellar pocket. In search for new bi-lobe proteins, comparative proteomics was performed and a leucine-rich repeats containing protein, TbLRRP1, was characterized as a new bi-lobe component. Inducible depletion of TbLRRP1 by RNA interference inhibited duplication of the bi-lobe as well as the adjacent Golgi apparatus and flagellar pocket collar. Formation of a new flagellum attachment zone and subsequent cell division were also inhibited. TbLRRP1 was used as a bi-lobe specific marker for immunoisolation of the bi-lobe complex. Among >70 candidates obtained from MS analyses of the immunoisolated bi-lobe, we focused on four candidates: BB50, FP45, p197 and TbSpef. These proteins provided new markers to follow T. brucei organelle biogenesis and inheritance. They also confirmed the presence of an extensive connection among the single-copied organelles in T. brucei.
URI: http://scholarbank.nus.edu.sg/handle/10635/43569
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