A ratchet-like inter-subunit reorganization of the ribosome during translocation
Abstract
The ribosome is a macromolecular assembly that is responsible for protein biosynthesis following genetic instructions in all organisms. It is composed of two unequal subunits: the smaller subunit binds messenger RNA and the anticodon end of transfer RNAs, and helps to decode the mRNA; and the larger subunit interacts with the amino-acid-carrying end of tRNAs and catalyses the formation of the peptide bonds. After peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, triggering the translocation of peptidyl-tRNA from its aminoacyl site to the peptidyl site, and movement of mRNA by one codon. Here we analyse three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states, and show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S subunit relative to the large 50S subunit. Furthermore, our finding indicates a two-step mechanism of translocation: first, relative rotation of the subunits and opening of the mRNA channel following binding of GTP to EF-G; and second, advance of the mRNA/(tRNA)2 complex in the direction of the rotation of the 30S subunit, following GTP hydrolysis.
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The part of H44 to which HygB binds has been implicated in movements during translocation.
“The part of H44 to which HygB binds has recently been implicated in movements during translocation (Frank and Agrawal 2000”
From The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit (2000) · cites this paper as Frank and Agrawal 2000
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- Authors
- Frank, J., & Agrawal, R. K.
- Affiliations
- State University of New York (US)
- Venue
- Nature
- Published
- 2000-07
- Volume
- 406
- Issue
- 6793
- Pages
- 318-322
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1677689941
- Cited by
- 799
- References
- 0
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 13 · 2023: 20 · 2022: 22 · 2021: 19 · 2020: 24 · 2019: 20 · 2018: 14 · 2017: 29 · 2016: 32 · 2015: 41 · 2014: 39 · 2013: 43 · 2012: 38
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- ribosome, translocation, elongation factor G, GTP hydrolysis, 70S ribosome, Escherichia coli, peptide bond formation, protein synthesis, cryo-electron microscopy
- MeSH terms
- Biological Transport, Escherichia coli, Guanosine Triphosphate, Hydrolysis, Models, Molecular, Molecular Conformation, Ribosomes, RNA, Messenger, RNA, Transfer, Cryoelectron Microscopy, Peptide Elongation Factor G, Macromolecular Substances
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