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  Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY.

Lakomek, N. A., Draycheva, A., Bornemann, T., & Wintermeyer, W. (2016). Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY. Angewandte Chemie International Edition, 55(33), 9544-9547. doi:10.1002/anie.201602905.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-F31C-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-66FC-D
Genre: Journal Article

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 Creators:
Lakomek, N. A., Author
Draycheva, A.1, Author              
Bornemann, T.2, Author              
Wintermeyer, W.2, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

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Free keywords: NMR spectroscopy; biophysics; intrinsically disordered proteins; protein-protein interactions; translocon
 Abstract: Integral membrane proteins in bacteria are co-translationally targeted to the SecYEG translocon for membrane insertion via the signal recognition particle (SRP) pathway. The SRP receptor FtsY and its N-terminal A domain, which is lacking in any structural model of FtsY, were studied using NMR and fluorescence spectroscopy. The A domain is mainly disordered and highly flexible; it binds to lipids via its N terminus and the C-terminal membrane targeting sequence. The central A domain binds to the translocon non-specifically and maintains disorder. Translocon targeting and binding of the A domain is driven by electrostatic interactions. The intrinsically disordered A domain tethers FtsY to the translocon, and because of its flexibility, allows the FtsY NG domain to scan a large area for binding to the NG domain of ribosome-bound SRP, thereby promoting the formation of the quaternary transfer complex at the membrane.

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Language(s): eng - English
 Dates: 2016-06-272016-08-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201602905
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 55 (33) Sequence Number: - Start / End Page: 9544 - 9547 Identifier: -