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Science. 2001 Apr 20;292(5516):453-4.
Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.
Evologic SA, 4 rue Pierre Fontaine, 91000 Evry, France.
Aminoacyl transfer RNA (tRNA) synthetases establish the rules of the genetic code by catalyzing the aminoacylation of tRNAs. For some synthetases, accuracy depends critically on an editing function at a site distinct from the aminoacylation site. Mutants of Escherichia coli that incorrectly charge tRNA(Val) with cysteine were selected after random mutagenesis of the whole chromosome. All mutations obtained were located in the editing site of valyl-tRNA synthetase. More than 20% of the valine in cellular proteins from such an editing mutant organism could be replaced with the noncanonical aminobutyrate, sterically similar to cysteine. Thus, the editing function may have played a central role in restricting the genetic code to 20 amino acids. Disabling this editing function offers a powerful approach for diversifying the chemical composition of proteins and for emulating evolutionary stages of ambiguous translation.
PMID: 11313495 [PubMed - indexed for MEDLINE]
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Cited by 24 PubMed Central articles
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Quality control despite mistranslation caused by an ambiguous genetic code.
Ruan B, Palioura S, Sabina J, Marvin-Guy L, Kochhar S, Larossa RA, Söll D.
Proc Natl Acad Sci U S A. 2008 Oct 28; 105(43):16502-7. Epub 2008 Oct 22.
[Proc Natl Acad Sci U S A. 2008]
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ReviewAminoacyl tRNA synthetases and their connections to disease.
Park SG, Schimmel P, Kim S.
Proc Natl Acad Sci U S A. 2008 Aug 12; 105(32):11043-9. Epub 2008 Aug 5.
[Proc Natl Acad Sci U S A. 2008]
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In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity.
Splan KE, Musier-Forsyth K, Boniecki MT, Martinis SA.
Methods. 2008 Feb; 44(2):119-28.
[Methods. 2008]
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