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Dynamic switch of the signal recognition particle from scanning to targeting.

MPG-Autoren
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Holtkamp,  W.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Lee,  S.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Bornemann,  T.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Senyushkina,  T.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

Volltexte (frei zugänglich)

1587305.pdf
(Verlagsversion), 569KB

Ergänzendes Material (frei zugänglich)

1587305-Suppl.pdf
(Ergänzendes Material), 2MB

Zitation

Holtkamp, W., Lee, S., Bornemann, T., Senyushkina, T., Rodnina, M. V., & Wintermeyer, W. (2012). Dynamic switch of the signal recognition particle from scanning to targeting. Nature Structural and Molecular Biology, 19(12), 1332-1337. doi:10.1038/nsmb.2421.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-000E-7064-1
Zusammenfassung
Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show that after initial binding to the ribosome, SRP undergoes dynamic fluctuations in search of additional interactions. Non-translating ribosomes, or ribosomes synthesizing non-membrane proteins, do not provide these contacts, allowing SRPs to dissociate rapidly. A nascent peptide in the exit tunnel stabilizes SRPs in a standby state. Binding to the emerging signal-anchor sequence (SAS) of a nascent membrane protein halts the fluctuations of SRP, resulting in complex stabilization and recruitment of the SRP receptor. We propose a kinetic model where SRP rapidly scans all ribosomes until it encounters a ribosome exposing an SAS. Binding to the SAS switches SRP into the targeting mode, in which dissociation is slow and docking of the SRP receptor is accelerated.