Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome

Ahmad Jomaa, Yu-Hsien Hwang Fu, Daniel Boehringer, Marc Leibundgut, Shu-ou Shan and Nenad Ban ()
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Ahmad Jomaa: Institute of Molecular Biology and Biophysics
Yu-Hsien Hwang Fu: California Institute of Technology
Daniel Boehringer: Institute of Molecular Biology and Biophysics
Marc Leibundgut: Institute of Molecular Biology and Biophysics
Shu-ou Shan: California Institute of Technology
Nenad Ban: Institute of Molecular Biology and Biophysics

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the membrane, where the signal peptide is transferred to the translocon. Using electron cryo-microscopy, we have determined the structure of a quaternary complex of the translating Escherichia coli ribosome, the SRP–SR in the ‘activated’ state and the translocon. Our structure, supported by biochemical experiments, reveals that the SRP RNA adopts a kinked and untwisted conformation to allow repositioning of the ‘activated’ SRP–SR complex on the ribosome. In addition, we observe the translocon positioned through interactions with the SR in the vicinity of the ribosome exit tunnel where the signal sequence is extending beyond its hydrophobic binding groove of the SRP M domain towards the translocon. Our study provides new insights into the mechanism of signal sequence transfer from the SRP to the translocon.

Date: 2017
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DOI: 10.1038/ncomms15470

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