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Quality control of substrate conformation in the Escherichia coli Twin Arginine protein-targeting pathway

Mermans, Daphne Maria Johanna (2018) Quality control of substrate conformation in the Escherichia coli Twin Arginine protein-targeting pathway. Doctor of Philosophy (PhD) thesis, University of Kent,. (KAR id:69592)

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Abstract

In Escherichia coli, the twin arginine translocase (Tat) is one of the major protein

across the inner membrane. Therefore, it has the ability to discriminate between folding

substrate. In this study we probed the Tat proofreading mechanism and we investigated

folding kinetics. We demonstrate that the E. coli Tat machinery can process a de-novo designed substrate

different folding states of this substrate. This data and the fact that this simple four helix

candidate to study the Tat proofreading mechanism (chapter 3).

surfaces of BT6 maquette. Mutants with substituted surface properties were expressed in

mutants were accepted or rejected by Tat. We propose that the proofreading system does

unfolded regions. Finally, we tested whether Tat substrates fold co- or post-translationally to determine the

(chapter 5). This study was to increase our understanding about the rationale for using the

Tat system.

Item Type: Thesis (Doctor of Philosophy (PhD))
Thesis advisor: Robinson, Colin
Divisions: Faculties > Sciences > School of Biosciences
SWORD Depositor: System Moodle
Depositing User: System Moodle
Date Deposited: 16 Oct 2018 11:11 UTC
Last Modified: 23 Jan 2020 04:15 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/69592 (The current URI for this page, for reference purposes)
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