Turner, Raymond JosephLevchenko, Elina2019-09-172019-09-172019-09-12Levchenko, 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.http://hdl.handle.net/1880/110985Tat-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.engUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.TATprotein translocationredox enzyme maturation proteinstwin-arginine translocationdifferential scanning fluorimetrycircular dichroismBiochemistrymaster thesis10.11575/PRISM/37050