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  The bacterial SRP receptor, FtsY, is activated on binding to the translocon.

Draycheva, A., Bornemann, T., Ryazanov, S., Lakomek, N. A., & Wintermeyer, W. (2016). The bacterial SRP receptor, FtsY, is activated on binding to the translocon. Molecular Microbiology, 102(1), 152-167. doi:10.1111/mmi.13452.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-FFEE-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-A358-E
Genre: Journal Article

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 Creators:
Draycheva, A.1, Author              
Bornemann, T.2, Author              
Ryazanov, S.3, Author              
Lakomek, N. A.3, 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              
3Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: FRET; NMR spectroscopy; SRP receptor; membrane targeting; site-directed crosslinking; translocon
 Abstract: Proteins are inserted into the bacterial plasma membrane cotranslationally after translating ribosomes are targeted to the translocon in the membrane via the signal recognition particle (SRP) pathway. The targeting pathway involves an interaction between SRP and the SRP receptor, FtsY. Here we focus on the role of FtsY and its interaction with the translocon in controlling targeting. We show that in unbound FtsY the NG and A domains interact with one another. The interaction involves the membrane-targeting region at the junction between A and N domain. The closed form of FtsY is impaired in binding to SRP. Upon binding to the phospholipid-embedded translocon the domains of FtsY move apart. This enhances the docking of the FtsY NG domain to the homologous NG domain of the SRP protein Ffh. Thus, FtsY binding to the translocon has a central role in orchestrating the formation of a quaternary transfer complex in which the nascent peptide is transferred to the translocon. We propose that FtsY activation at the translocon ensures that ribosome-SRP complexes are directed to available translocons. This way sequestering SRP in futile complexes with unbound FtsY can be avoided and efficient targeting to the translocon achieved

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Language(s): eng - English
 Dates: 2016-07-192016-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1111/mmi.13452
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Title: Molecular Microbiology
Source Genre: Journal
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Pages: - Volume / Issue: 102 (1) Sequence Number: - Start / End Page: 152 - 167 Identifier: -