Characterization of interactions between DmsD, DmsA, and TatB for the docking step for the bacterial twin-arginine translocase
Date
2019-09-12
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Abstract
Tat-pathway is the primary translocation system which deals with fully-folded proteins that all bear a “twin arginine” motif with a consensus sequence S/TRRXFLK. Three major Escherichia coli components are TatA, TatB and TatC, where the last two comprise a functional unit responsible for cargo docking. My project utilized a heterotrimer Dimethyl Sulfoxide (DMSO) reductase as a model system with two constituents (DmsA and DmsB) requiring assistance from a DmsD chaperone to reach the translocon. My goal was to study the order of events during the docking of DmsA onto the TatB and potential involvement of DmsD. The work supports that DmsD mediates the PMF-dependent transfer of the substrate to the translocase system. It was also shown in vitro (differential scanning fluorimetry; circular dichroism; chromatography) and in silico that DmsD has binding sites on its surface for DmsA and TatB, and they are distinct and potentially regulated by Mg2+ and GNP.
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Keywords
TAT, protein translocation, redox enzyme maturation proteins, twin-arginine translocation, differential scanning fluorimetry, circular dichroism
Citation
Levchenko, E. (2019). Characterization of interactions between DmsD, DmsA, and TatB for the docking step for the bacterial twin-arginine translocase (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca.