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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Winstone, Tara M. L. Turner, Raymond J. Kuzniatsova, Lalita |
| Description | Author Affiliation: Kuzniatsova L ( Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Alberta T2N 1N4, Canada.); Winstone TM ( Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Alberta T2N 1N4, Canada.); Turner RJ ( Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Alberta T2N 1N4, Canada. Electronic address: turnerr@ucalgary.ca.) |
| Abstract | The Twin-arginine translocation (Tat) pathway serves for translocation of fully folded proteins across the cytoplasmic membrane in bacterial and chloroplast thylakoid membranes. The Escherichia coli Tat system consists of three core components: TatA, TatB, and TatC. The TatB and TatC subunits form the receptor complex for Tat dependent proteins. The TatB protein is composed of a single transmembrane helix and cytoplasmic domain. The structure of TatC revealed six transmembrane helices. Redox Enzyme Maturation Proteins (REMPs) are system specific chaperones, which play roles in the maturation of Tat dependent respiratory enzymes. Here we applied the in vivo bacterial two-hybrid technique to investigate interaction of REMPs with the TatBC proteins, finding that all but the formate dehydrogenase REMP dock to TatB or TatC. We focused on the NarJ subfamily, where DmsD – the REMP for dimethyl sulfoxide reductase in E. coli – was previously shown to interact with TatB and TatC. We found that these REMPs interact with TatC cytoplasmic loops 1, 2 and 4, with the exception of NarJ, that only interacts with 1 and 4. An in vitro isothermal titration calorimetry study was applied to confirm the evidence of interactions between TatC fragments and DmsD chaperone. Using a peptide overlapping array, it was shown that the different NarJ subfamily REMPs interact with different regions of the TatB cytoplasmic domains. The results demonstrate a role of REMP chaperones in targeting respiratory enzymes to the Tat system. The data suggests that the different REMPs may have different mechanisms for this task. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1858 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Cell Membrane Chemistry Escherichia Coli Proteins Membrane Transport Proteins Molecular Chaperones Carrier Proteins Metabolism Escherichia Coli Enzymology Formate Dehydrogenases Protein Folding Protein Interaction Maps Protein Structure, Tertiary Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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