Coupling of Ribosomal L1 Stalk and tRNA Dynamics during Translation Elongation
Open accessAbstract
By using single-molecule fluorescence resonance energy transfer (smFRET), we observe the real-time dynamic coupling between the ribosome, labeled at the L1 stalk, and transfer RNA (tRNA). We find that an interaction between the ribosomal L1 stalk and the newly deacylated tRNA is established spontaneously upon peptide bond formation; this event involves coupled movements of the L1 stalk and tRNAs as well as ratcheting of the ribosome. In the absence of elongation factor G, the entire pretranslocation ribosome fluctuates between just two states: a nonratcheted state, with tRNAs in their classical configuration and no L1 stalk-tRNA interaction, and a ratcheted state, with tRNAs in an intermediate hybrid configuration and a direct L1 stalk-tRNA interaction. We demonstrate that binding of EF-G shifts the equilibrium toward the ratcheted state. Real-time smFRET experiments reveal that the L1 stalk-tRNA interaction persists throughout the translocation reaction, suggesting that the L1 stalk acts to direct tRNA movements during translocation.
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GTP hydrolysis induces substantial conformational changes in the ribosome.
“It is known that GTP hydrolysis induces substantial conformational changes in the ribosome.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [23]
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- Authors
- Fei, J., Kosuri, P., MacDougall, D. D., & Gonzalez, R. L.
- Affiliations
- Columbia University (US)
- Corresponding author
- Gonzalez, Ruben L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 30
- Issue
- 3
- Pages
- 348-359
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2080720176
- Cited by
- 316
- References
- 29
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 10 · 2023: 11 · 2022: 14 · 2021: 13 · 2020: 7 · 2019: 8 · 2018: 16 · 2017: 20 · 2016: 23 · 2015: 19 · 2014: 29 · 2013: 24 · 2012: 26
- FWCI
- 11.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- National Institute of General Medical Sciences (R01GM084288)
- 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 › Molecular Biology › Protein Structure and Dynamics
- Keywords
- translation elongation, ribosome translocation, elongation factor G, peptide bond formation, single-molecule FRET
- MeSH terms
- Carbocyanines, Fluorescent Dyes, Models, Molecular, Nucleic Acid Conformation, Peptide Chain Elongation, Translational, Protein Conformation, Ribosomal Proteins, Ribosomes, RNA, Transfer, Fluorescence Resonance Energy Transfer, Macromolecular Substances
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