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Assembling the Tat protein translocase.
| Content Provider | Europe PMC |
|---|---|
| Author | Alcock, Felicity Stansfeld, Phillip J Basit, Hajra Habersetzer, Johann Baker, Matthew AB Palmer, Tracy Wallace, Mark I Berks, Ben C |
| Editor | Ben-Tal, Nir |
| Copyright Year | 2016 |
| Abstract | The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes.DOI: http://dx.doi.org/10.7554/eLife.20718.001 |
| Journal | eLife |
| Volume Number | 5 |
| PubMed Central reference number | PMC5201420 |
| PubMed reference number | 27914200 |
| e-ISSN | 2050084X |
| DOI | 10.7554/elife.20718 |
| Language | English |
| Publisher | eLife Sciences Publications, Ltd |
| Publisher Date | 2016-12-03 |
| Access Restriction | Open |
| Rights License | This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. © 2016, Alcock et al |
| Subject Keyword | Tat protein transport sequence co-evolution membrane protein twin-arginine E. coli |
| Content Type | Text |
| Resource Type | Article |
| Subject | Immunology and Microbiology Neuroscience Medicine Biochemistry, Genetics and Molecular Biology |
