Characterization of interactions between DmsD, DmsA, and TatB  for the docking step for the bacterial twin-arginine translocase

Levchenko, Elina

Characterization of interactions between DmsD, DmsA, and TatB for the docking step for the bacterial twin-arginine translocase

dc.contributor.advisor	Turner, Raymond Joseph
dc.contributor.author	Levchenko, Elina
dc.contributor.committeemember	Noskov, Sergei Yu
dc.contributor.committeemember	Moorhead, Greg B. G.
dc.date	2019-11
dc.date.accessioned	2019-09-17T14:17:57Z
dc.date.available	2019-09-17T14:17:57Z
dc.date.issued	2019-09-12
dc.description.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.	en_US
dc.identifier.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.	en_US
dc.identifier.doi	http://dx.doi.org/10.11575/PRISM/37050
dc.identifier.uri	http://hdl.handle.net/1880/110985
dc.language.iso	eng	en_US
dc.publisher.faculty	Science	en_US
dc.publisher.institution	University of Calgary	en
dc.rights	University 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.	en_US
dc.subject	TAT	en_US
dc.subject	protein translocation	en_US
dc.subject	redox enzyme maturation proteins	en_US
dc.subject	twin-arginine translocation	en_US
dc.subject	differential scanning fluorimetry	en_US
dc.subject	circular dichroism	en_US
dc.subject.classification	Biochemistry	en_US
dc.title	Characterization of interactions between DmsD, DmsA, and TatB for the docking step for the bacterial twin-arginine translocase	en_US
dc.type	master thesis	en_US
thesis.degree.discipline	Biological Sciences	en_US
thesis.degree.grantor	University of Calgary	en_US
thesis.degree.name	Master of Science (MSc)	en_US
ucalgary.item.requestcopy	true	en_US