The twin arginine tranlocation (Tat) pathway is responsible for the transport of folded protein across the membrane. In bacteria, this occurs at the cytoplasmic membrane. In Gram-negative bacteria, Tat forms a 3-component machinery named TatABC. The current hypothesised mechanism is compiled from the model organism Escherichia coli. In Gram-positive bacteria the Tat machinery lack the TatB component and so raises the question on the validity of the mechanism assumed from the TatABC system. To date there is limited research available on the TatAC system with in Gram-postive bacteria. Recent characterisation has been focused on the Bacillus subtilis system, which contain two TatAC systems; the TatAdCd and TatAyCy. This thesis focuses on the structural characterisation of the TatAC system of B. subtilis and their similarity to the TatABC system in E. coli. The TatAdCd complex was studies by electron microscopy (EM) to show structure similarity to the TatBC complex. Mutation within the N-terminus region of the TatAy protein showed functional involved in complex assembly. The TatAyCy was also analysed by EM show conserved round complexes similar to the TatAdCd and TatBC. The similarity in structure may suggest the Gram-negatives and the Gram-Positives share a similar mechanism of transport despite difference in the components.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:629110 |
| Date | January 2014 |
| Creators | Patel, Roshani |
| Publisher | University of Warwick |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://wrap.warwick.ac.uk/63783/ |
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