In vivo experiments do not support the charge zipper model for Tat translocase assembly
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...
Main Authors: | Alcock, F, Damen, M, Levring, J, Berks, B |
---|---|
Format: | Journal article |
Published: |
eLife Sciences Publications
2017
|
Similar Items
-
In vivo experiments do not support the charge zipper model for Tat translocase assembly
by: Felicity Alcock, et al.
Published: (2017-08-01) -
Assembling the tat protein translocase
by: Alcock, F, et al.
Published: (2016) -
Assembling the Tat protein translocase
by: Alcock, F, et al.
Published: (2016) -
Assembling the Tat protein translocase
by: Felicity Alcock, et al.
Published: (2016-12-01) -
New insights into the Tat protein transport cycle from characterising the assembled Tat translocon
by: Alcock, F, et al.
Published: (2022)