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Journal Article

Structures of ribosome-bound initiation factor 2 reveal mechanism of subunit association

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Bürger,  Jörg
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;
1Institut für Medizinische Physik und Biophysik, Charité–Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany;

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Mielke,  Thorsten
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;
1Institut für Medizinische Physik und Biophysik, Charité–Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany;

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Citation

Sprink, T., Ramrath, D. J. F., Yamamoto, H., Yamamoto, K., Loerke, J., Ismer, J., et al. (2016). Structures of ribosome-bound initiation factor 2 reveal mechanism of subunit association. Science Advances, 2(3): e1501502. doi:10.1126/sciadv.1501502.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-44E0-F
Abstract
Throughout the four phases of protein biosynthesis—initiation, elongation, termination, and recycling—the ribosome is controlled and regulated by at least one specified translational guanosine triphosphatase (trGTPase). Although the structural basis for trGTPase interaction with the ribosome has been solved for the last three steps of translation, the high-resolution structure for the key initiation trGTPase, initiation factor 2 (IF2), complexed with the ribosome, remains elusive. We determine the structure of IF2 complexed with a nonhydrolyzable guanosine triphosphate analog and initiator fMet-tRNAiMet in the context of the Escherichia coli ribosome to 3.7-Å resolution using cryo-electron microscopy. The structural analysis reveals previously unseen intrinsic conformational modes of the 70S initiation complex, establishing the mutual interplay of IF2 and initator transfer RNA (tRNA) with the ribsosome and providing the structural foundation for a mechanistic understanding of the final steps of translation initiation.