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-Structure paper
Title | EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 21, Issue 2, Page 152-159, Year 2014 |
Publish date | Jan 5, 2014 |
Authors | Bo Chen / Grégory Boël / Yaser Hashem / Wei Ning / Jingyi Fei / Chi Wang / Ruben L Gonzalez / John F Hunt / Joachim Frank / |
PubMed Abstract | Cells express many ribosome-interacting factors whose functions and molecular mechanisms remain unknown. Here, we elucidate the mechanism of a newly characterized regulatory translation factor, ...Cells express many ribosome-interacting factors whose functions and molecular mechanisms remain unknown. Here, we elucidate the mechanism of a newly characterized regulatory translation factor, energy-dependent translational throttle A (EttA), which is an Escherichia coli representative of the ATP-binding cassette F (ABC-F) protein family. Using cryo-EM, we demonstrate that the ATP-bound form of EttA binds to the ribosomal tRNA-exit site, where it forms bridging interactions between the ribosomal L1 stalk and the tRNA bound in the peptidyl-tRNA-binding site. Using single-molecule fluorescence resonance energy transfer, we show that the ATP-bound form of EttA restricts ribosome and tRNA dynamics required for protein synthesis. This work represents the first example, to our knowledge, in which the detailed molecular mechanism of any ABC-F family protein has been determined and establishes a framework for elucidating the mechanisms of other regulatory translation factors. |
External links | Nat Struct Mol Biol / PubMed:24389465 / PubMed Central |
Methods | EM (single particle) |
Resolution | 7.5 - 9.1 Å |
Structure data | EMDB-5784: EttA-bound E. coli 70S ribosome complex containing P-site tRNA and A-site tRNA EMDB-5785: EMDB-5786: EMDB-5841: EMDB-5842: EMDB-5843: |
Source |
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Keywords | RIBOSOME/TRANSLATION / protein translation regulation / ABC-F protein family / single-molecule FRET / YjjK / RIBOSOME-TRANSLATION complex |