Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites - Wikidata - awgldk - TriplyDB

Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites

Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites

http://www.wikidata.org/entity/Q34186873

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Carbon source-dependent expansion of the genetic code in bacteria The Impact of Non-Enzymatic Reactions and Enzyme Promiscuity on Cellular Metabolism during (Oxidative) Stress Conditions Molecular basis for population variation: from SNPs to SAPs The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.Mistranslation can enhance fitness through purging of deleterious mutations.tRNA synthetase: tRNA aminoacylation and beyond Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code Adaptive translation as a mechanism of stress response and adaptation.Exploring the substrate range of wild-type aminoacyl-tRNA synthetases.A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity Amino-acid-dependent shift in tRNA synthetase editing mechanisms.Coordination of tRNA synthetase active sites for chemical fidelity Low level genome mistranslations deregulate the transcriptome and translatome and generate proteotoxic stress in yeast.Mistranslation of the genetic code.Protein aggregation caused by aminoglycoside action is prevented by a hydrogen peroxide scavenger.Protein mistranslation protects bacteria against oxidative stress Predicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes.Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.MIST, a Novel Approach to Reveal Hidden Substrate Specificity in Aminoacyl-tRNA Synthetases.Structural analyses clarify the complex control of mistranslation by tRNA synthetases Methionine Mistranslation Bypasses the Restraint of the Genetic Code to Generate Mutant Proteins with Distinct Activities.Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology.Decoding in Candidatus Riesia pediculicola, close to a minimal tRNA modification set?Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code.Translation quality control is critical for bacterial responses to amino acid stress.Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK Capture and quality control mechanisms for adenosine-5'-triphosphate binding.Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase Reversion of a fungal genetic code alteration links proteome instability with genomic and phenotypic diversification.Reduced Protein Synthesis Fidelity Inhibits Flagellar Biosynthesis and Motility.Structural characterization of antibiotic self-immunity tRNA synthetase in plant tumour biocontrol agent.Quality Control by Isoleucyl-tRNA Synthetase of Bacillus subtilis Is Required for Efficient Sporulation.Emergence and evolution.Transfer RNA: a dancer between charging and mis-charging for protein biosynthesis.Rescuing discarded spectra: Full comprehensive analysis of a minimal proteome.

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P2860

Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites

http://www.wikidata.org/entity/Q34186873

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Brian S Imai

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Jacob D Jaffe

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Li Li

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Michal T Boniecki

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Peter M Yau

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Susan A Martinis

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Zaida A Luthey-Schulten

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The complete genome and proteome of Mycoplasma mobile

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

On the evolution of cells

Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase

The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue

RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models

Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration

MultiSeq: unifying sequence and structure data for evolutionary analysis.

Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro.

Cell-specific differences in the requirements for translation quality control

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