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Repurposing tRNAs f...
Repurposing tRNAs for nonsense suppression
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- Albers, Suki (author)
- Univ Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany.
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- Beckert, Bertrand (author)
- Univ Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany.
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- Matthies, Marco C. (author)
- Univ Hamburg, Ctr Bioinformat, Hamburg, Germany.
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- Mandava, Chandra Sekhar, 1978- (author)
- Uppsala universitet,Molekylärbiologi
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- Schuster, Raphael (author)
- Univ Hamburg, Inst Organ Chem, Hamburg, Germany.
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- Seuring, Carolin (author)
- Ctr Struct & Syst Biol, Hamburg, Germany.
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- Riedner, Maria (author)
- Univ Hamburg, Inst Organ Chem, Hamburg, Germany.
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- Sanyal, Suparna (author)
- Uppsala universitet,Molekylärbiologi
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- Torda, Andrew E. (author)
- Univ Hamburg, Ctr Bioinformat, Hamburg, Germany.
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- Wilson, Daniel N. (author)
- Univ Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany.
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- Ignatova, Zoya (author)
- Univ Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany.
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Univ Hamburg, Inst Biochem & Mol Biol, Hamburg, Germany Univ Hamburg, Ctr Bioinformat, Hamburg, Germany. (creator_code:org_t)
- 2021-06-22
- 2021
- English.
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In: Nature Communications. - : Springer Nature. - 2041-1723. ; 12
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Abstract
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- Three stop codons (UAA, UAG and UGA) terminate protein synthesis and are almost exclusively recognized by release factors. Here, we design de novo transfer RNAs (tRNAs) that efficiently decode UGA stop codons in Escherichia coli. The tRNA designs harness various functionally conserved aspects of sense-codon decoding tRNAs. Optimization within the T Psi C-stem to stabilize binding to the elongation factor, displays the most potent effect in enhancing suppression activity. We determine the structure of the ribosome in a complex with the designed tRNA bound to a UGA stop codon in the A site at 2.9 angstrom resolution. In the context of the suppressor tRNA, the conformation of the UGA codon resembles that of a sense-codon rather than when canonical translation termination release factors are bound, suggesting conformational flexibility of the stop codons dependent on the nature of the A-site ligand. The systematic analysis, combined with structural insights, provides a rationale for targeted repurposing of tRNAs to correct devastating nonsense mutations that introduce a premature stop codon. Here, the authors report de novo design, optimization and characterization of tRNAs that decode UGA stop codons in E. coli. The structure of the ribosome in a complex with the designed tRNA bound to a UGA stop codon suggests that distinct A-site ligands (tRNAs versus release factors) induce distinct conformation of the stop codon within the mRNA in the decoding center.
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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- By the author/editor
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Albers, Suki
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Beckert, Bertran ...
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Matthies, Marco ...
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Mandava, Chandra ...
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Schuster, Raphae ...
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Seuring, Carolin
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show more...
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Riedner, Maria
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Sanyal, Suparna
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Torda, Andrew E.
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Wilson, Daniel N ...
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Ignatova, Zoya
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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Nature Communica ...
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Uppsala University