ArticleProceedings of the National Academy of Sciences of the United States of America2003
Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.Nature communications · 2025Article
- Topological analyses of the L-lysine exporter LysO reveal a critical role for a conserved pair of intramembrane solvent-exposed acidic residues.The Journal of biological chemistry · 2021Article
- Interrogating Genes That Mediate Chlamydia trachomatis Survival in Cell Culture Using Conditional Mutants and Recombination.Journal of bacteriology · 2016Article
- A Member of the Arabidopsis Mitochondrial Transcription Termination Factor Family Is Required for Maturation of Chloroplast Transfer RNAIle(GAU).Plant physiology · 2015Article
- Proline responding1 Plays a Critical Role in Regulating General Protein Synthesis and the Cell Cycle in Maize.The Plant cell · 2014Article
- Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide.Nature communications · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Site-specific fatty acid-conjugation to prolong protein half-life in vivo.Journal of controlled release : official journal of the Controlled Release Society · 2013Article
- Importance of adenosine-to-inosine editing adjacent to the anticodon in an Arabidopsis alanine tRNA under environmental stress.Nucleic acids research · 2013Article
- Downward causation by information control in micro-organisms.Interface focus · 2012Article
- Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes.The Journal of biological chemistry · 2011Article
- The T box regulatory element controlling expression of the class I lysyl-tRNA synthetase of Bacillus cereus strain 14579 is functional and can be partially induced by reduced charging of asparaginyl-tRNAAsn.BMC microbiology · 2010Article
- Non-antibiotic selection systems for soybean somatic embryos: the lysine analog aminoethyl-cysteine as a selection agent.BMC biotechnology · 2009Article
- Mechanisms of resistance to an amino acid antibiotic that targets translation.ACS chemical biology · 2007Article
- A natural genetic code expansion cassette enables transmissible biosynthesis and genetic encoding of pyrrolysine.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Discrimination of cognate and noncognate substrates at the active site of class I lysyl-tRNA synthetase.Biochemistry · 2006Article
- Enzymatic aminoacylation of tRNA with unnatural amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Paths of lateral gene transfer of lysyl-aminoacyl-tRNA synthetases with a unique evolutionary transition stage of prokaryotes coding for class I and II varieties by the same organisms.BMC evolutionary biology · 2006Article
- Article
- The CCA anticodon specifies separate functions inside and outside translation in Bacillus cereus.RNA biologyArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Insertion of lysine during protein synthesis depends on the enzyme lysyl-tRNA synthetase (LysRS), which exists in two unrelated forms, LysRS1 and LysRS2. LysRS1 has been found in most archaea and some bacteria, and LysRS2 has been found in eukarya, most bacteria, and a few archaea, but the two proteins are almost never found together in a single organism. Comparison of structures of LysRS1 and LysRS2 complexed with lysine suggested significant differences in their potential to bind lysine analogues with backbone replacements. One such naturally occurring compound, the metabolic intermediate S-(2-aminoethyl)-L-cysteine, is a bactericidal agent incorporated during protein synthesis via LysRS2. In vitro tests showed that S-(2-aminoethyl)-L-cysteine is a poor substrate for LysRS1, and that it inhibits LysRS1 200-fold less effectively than it inhibits LysRS2. In vivo inhibition by S-(2-aminoethyl)-L-cysteine was investigated by replacing the endogenous LysRS2 of Bacillus subtilis with LysRS1 from the Lyme disease pathogen Borrelia burgdorferi. B. subtilis strains producing LysRS1 alone were relatively insensitive to growth inhibition by S-(2-aminoethyl)-L-cysteine, whereas a WT strain or merodiploid strains producing both LysRS1 and LysRS2 showed significant growth inhibition under the same conditions. These growth effects arising from differences in amino acid recognition could contribute to the distribution of LysRS1 and LysRS2 in different organisms. More broadly, these data demonstrate how diversity of the aminoacyl-tRNA synthetases prevents infiltration of the genetic code by noncanonical amino acids, thereby providing a natural reservoir of potential antibiotic resistance.
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