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Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association
Author(s) -
Thiemo Sprink,
D.J.F. Ramrath,
Hiroshi Yamamoto,
Kaori Yamamoto,
Justus Loerke,
Jochen Ismer,
Peter W. Hildebrand,
Patrick Scheerer,
Jörg Bürger,
Thorsten Mielke,
Christian M. T. Spahn
Publication year - 2016
Publication title -
science advances
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.928
H-Index - 146
ISSN - 2375-2548
DOI - 10.1126/sciadv.1501502
Subject(s) - initiation factor , ribosome , eukaryotic translation , transfer rna , eukaryotic initiation factor , translation (biology) , internal ribosome entry site , guanosine , biophysics , microbiology and biotechnology , chemistry , biology , biochemistry , crystallography , rna , messenger rna , gene
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

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