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The structural basi...
The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy
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- Fu, Ziao (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, USA
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- Indrisiunaite, Gabriele (author)
- Uppsala universitet,Molekylärbiologi
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- Kaledhonkar, Sandip (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, USA
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- Shah, Binita (author)
- Department of Biological Sciences, Barnard College, New York, USA
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- Sun, Ming (author)
- Department of Biological Sciences, Colmbia University, New York, USA
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- Chen, Bo (author)
- Department of Biological Sciences, Colmbia University, New York, USA
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- Grassucci, Robert A. (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, USA
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- Ehrenberg, Måns (author)
- Uppsala universitet,Molekylärbiologi
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- Frank, Joachim (author)
- Department of Biochemistry and Molecular Biophysics, Columbia University, New York, USA; Department of Biological Sciences, Colmbia University, New York, USA
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(creator_code:org_t)
- 2019-06-12
- 2019
- English.
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In: Nature Communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 10
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Abstract
Subject headings
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- When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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