Journal article
In vivo experiments do not support the charge zipper model for Tat translocase assembly
- Abstract:
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The twin-arginine translocase (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat translocation site is formed by substrate-triggered oligomerization of the protein TatA. Walther and co-workers have proposed a structural model for the TatA oligomer in which TatA monomers self-assemble using electrostatic ‘charge zippers’ (Cell (2013) 132: 15945). This model was supported by in vitro analysis of the oligomeric state of TatA varia...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(pdf, 1.1MB)
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- Publisher copy:
- 10.7554/eLife.30127
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Authors
Bibliographic Details
- Publisher:
- eLife Sciences Publications Publisher's website
- Journal:
- eLife Journal website
- Volume:
- 6
- Article number:
- e30127
- Publication date:
- 2017-08-31
- Acceptance date:
- 2017-08-31
- DOI:
- EISSN:
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2050-084X
Item Description
- Keywords:
- Pubs id:
-
pubs:724708
- UUID:
-
uuid:0aedd4c6-655f-4e23-859b-c214f09f4502
- Local pid:
- pubs:724708
- Deposit date:
- 2017-08-31
Terms of use
- Copyright holder:
- Alcock et al
- Copyright date:
- 2017
- Notes:
- © 2017, Alcock et al. 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.
- Licence:
- CC Attribution (CC BY)
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