White Rose University Consortium logo
University of Leeds logo University of Sheffield logo York University logo

The Tripartite Tricarboxylate Transporters (TTT) : The neglected family of high-affinity uptake systems

Talachia Rosa, Leonardo (2018) The Tripartite Tricarboxylate Transporters (TTT) : The neglected family of high-affinity uptake systems. PhD thesis, University of Sheffield.

[img] Text
Thesis-LTR-2018-final.pdf
Restricted until 1 July 2023.

Request a copy
[img]
Preview
Text
Rosa.et.al.2018-Chapter1.pdf
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (3361Kb) | Preview
[img]
Preview
Text
Rosa.et.al.2018-Chapter4.pdf
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (3469Kb) | Preview
[img]
Preview
Text
Rosa.et.al.2017-Chapter5.pdf
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (1094Kb) | Preview
[img] Other (xlsx document)
Suplementary-material-Rosa.et.al.2018-Chapter1.xlsx
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (134Kb)
[img]
Preview
Text
Suplementary-material-Rosa.et.al.2018-Chapter4.pdf
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (1534Kb) | Preview
[img] Other (xlsx document)
Suplementary-material-Rosa.et.al.2018-Chapter4.xlsx
Available under License Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 UK: England & Wales.

Download (55Kb)

Abstract

Bacteria inhabiting complex environments must possess efficient ways of acquiring nutrients, often present in low concentrations. In this context, Solute Binding Protein (SBP) dependent transporters make use of a periplasmic binding protein to bind substrates with high affinity, and deliver them to their transmembrane counterparts. There are three known families of SBP dependent transporters: The ABC (ATP-Binding Cassette), the TRAP (TRipartite ATP-independent Periplasmic transporters) and the TTT (Tripartite Tricarboxylate Transporter). The latter are very poorly characterized and only a few types of substrates for TTT transporters are currently known. This thesis first presents a review of the TTT transporters. Our database searches reveal a massive overrepresentation of TTT SBPs among α and β-proteobacteria, and highlight the presence of 434 TTT SBPs in the bacterium Rhodoplanes sp. Z2-YC6860, the biggest gene family representation described in a bacterial genome to date. We subsequently focus on the characterization of the TTT family in Rhodopseudomonas palustris, a model soil non-sulfur purple bacterium. The TTT family in R. palustris is formed by two complete tripartite systems, plus five orphan SBPs with no obvious membrane counterparts. Two of the SBP were characterized biochemically and physiologically. One of the orphan SBPs (AdpC) is described to bind to dicarboxylic acids ranging from six to nine carbons in length with low µM affinity, and is more expressed under low concentration of adipate. A second SBP also had its binding properties and crystal structure characterised. In summary, this study presents a characterization of the Tripartite Tricarboxylate Transporter family in bacteria, through a synergistic multidisciplinary approach.

Item Type: Thesis (PhD)
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > Molecular Biology and Biotechnology (Sheffield)
Depositing User: Dr Leonardo Talachia Rosa
Date Deposited: 11 Sep 2018 08:29
Last Modified: 11 Sep 2018 08:29
URI: http://etheses.whiterose.ac.uk/id/eprint/21307

Some parts of this thesis can be downloaded immediately using the 'Download' link(s) above. Other parts can be requested by using the 'Request a copy' link(s) above.
You can contact us about this thesis. If you need to make a general enquiry, please see the Contact us page.

Actions (repository staff only: login required)