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Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry

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Kiosze-Becker, K., Ori, A., Gerovac, M., Heuer, A., Nürenberg-Goloub, E., Rashid, U. J., et al. (2016). Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry. Nature Communications, 7: 13248. doi:10.1038/ncomms13248.


Cite as: http://hdl.handle.net/21.11116/0000-0006-A815-5
Abstract
Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final-or the first-step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S·ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix-loop-helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling.