Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.629110
Title: Twin arginine translocase (Tat) : structural and functional insight
Author: Patel, Roshani
ISNI:       0000 0004 5348 2541
Awarding Body: University of Warwick
Current Institution: University of Warwick
Date of Award: 2014
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Abstract:
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.
Supervisor: Not available Sponsor: Medical Research Council
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.629110  DOI: Not available
Keywords: QR Microbiology
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