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In vivo experiments do not support the charge zipper model for Tat translocase assembly

Abstract:

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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Publisher copy:
10.7554/eLife.30127

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Oxford college:
Wadham College
Role:
Author
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:
2050-084X
Keywords:
Pubs id:
pubs:724708
UUID:
uuid:0aedd4c6-655f-4e23-859b-c214f09f4502
Local pid:
pubs:724708
Deposit date:
2017-08-31

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