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Lipids trigger a conformational switch that regulates Signal Recognition Particle (SRP)-mediated protein targeting

Co-translational protein targeting to the membrane is mediated by the signal recognition particle and its receptor (FtsY). Their homologous GTPase domains interact at the membrane and form a heterodimer in which both GTPases are activated. The prerequisite for protein targeting is the interaction of...

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Main Authors: Stjepanović, Goran (Author) , Kapp, Katja (Author) , Bange, Gert (Author) , Graf, Christian (Author) , Parlitz, Richard (Author) , Wild, Klemens (Author) , Mayer, Matthias P. (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 2011
In: The journal of biological chemistry
Year: 2011, Volume: 286, Issue: 26, Pages: 23489-23497
ISSN:1083-351X
DOI:10.1074/jbc.M110.212340
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M110.212340
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925819488820
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Author Notes:Goran Stjepanovic, Katja Kapp, Gert Bange, Christian Graf, Richard Parlitz, Klemens Wild, Matthias P. Mayer, and Irmgard Sinning
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Summary:Co-translational protein targeting to the membrane is mediated by the signal recognition particle and its receptor (FtsY). Their homologous GTPase domains interact at the membrane and form a heterodimer in which both GTPases are activated. The prerequisite for protein targeting is the interaction of FtsY with phospholipids. However, the mechanism of FtsY regulation by phospholipids remained unclear. Here we show that the N terminus of FtsY (A domain) is natively unfolded in solution and define the complete membrane-targeting sequence. We show that the membrane-targeting sequence is highly dynamic in solution, independent of nucleotides and directly responds to the density of anionic phospholipids by a random coil-helix transition. This conformational switch is essential for tethering FtsY to membranes and activates the GTPase for its subsequent interaction with the signal recognition particle. Our results underline the dynamics of lipid-protein interactions and their importance in the regulation of protein targeting and translocation across biological membranes.
Item Description:Online verfügbar 3 Mai 2011, Artikelversion 4 Januar 2021
Gesehen am 24.10.2022
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M110.212340

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