The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine - Wikidata - awgldk - TriplyDB

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

http://www.wikidata.org/entity/Q35226188

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Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)The tRNA-dependent biosynthesis of modified cyclic dipeptides Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability Novel genes associated with enhanced motility of Escherichia coli ST131.Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.The hypusine-containing translation factor eIF5A.Translation initiation rate determines the impact of ribosome stalling on bacterial protein synthesis.Genome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolution Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Polyspecific pyrrolysyl-tRNA synthetases from directed evolution Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani Predicting the minimal translation apparatus: lessons from the reductive evolution of mollicutes.β-Lysine discrimination by lysyl-tRNA synthetase.The large ribosomal subunit protein L9 enables the growth of EF-P deficient cells and enhances small subunit maturation Loss of elongation factor P disrupts bacterial outer membrane integrity Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa.(R)-β-lysine-modified elongation factor P functions in translation elongation.Global quantitative proteomics reveal up-regulation of endoplasmic reticulum stress response proteins upon depletion of eIF5A in HeLa cells.Translation Control of Swarming Proficiency in Bacillus subtilis by 5-Amino-pentanolylated Elongation Factor P eIF5A promotes translation of polyproline motifs.Deciphering the Translation Initiation Factor 5A Modification Pathway in Halophilic Archaea.Molecular evolution of protein-RNA mimicry as a mechanism for translational control Proteobacteria explain significant functional variability in the human gut microbiome.Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode.Emergence and evolution.eIF5A and EF-P: two unique translation factors are now traveling the same road.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology Rewiring protein synthesis: From natural to synthetic amino acids.Spermidine promotes Bacillus subtilis biofilm formation by activating expression of the matrix regulator slrR.Maintenance of protein synthesis reading frame by EF-P and m(1)G37-tRNA.Crystallization and preliminary X-ray crystallographic analysis of YfcM: an important factor for EF-P hydroxylation.Essential structural elements in tRNA(Pro) for EF-P-mediated alleviation of translation stalling.Elongation factor P is dispensable in Escherichia coli and Pseudomonas aeruginosa.EF-P dependent pauses integrate proximal and distal signals during translation.eIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer.EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.

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P2860

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

http://www.wikidata.org/entity/Q35226188

description

2011 nî lūn-bûn

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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

@ast

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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type

label

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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prefLabel

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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Nature Chemical Biology

P1476

The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

@en

P2093

Benjamin S Wolfe

http://www.w3.org/2001/XMLSchema#string

Craig J Forsyth

http://www.w3.org/2001/XMLSchema#string

Hervé Roy

http://www.w3.org/2001/XMLSchema#string

Marla S Gilreath

http://www.w3.org/2001/XMLSchema#string

Michael Ibba

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S Betty Zou

http://www.w3.org/2001/XMLSchema#string

Tammy J Bullwinkle

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P2860

Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate

Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70S Ribosome

PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella enterica

A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase

Hypusine-containing protein eIF5A promotes translation elongation

Adding new chemistries to the genetic code

Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

Aminoacyl-tRNA synthesis

Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis.

P2888

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667-669

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scholarly article

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10.1038/NCHEMBIO.632

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10

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7

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William Wiley Navarre

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2011-08-14T00:00:00Z

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51571626

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21841797

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3177975

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