A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27664126

about

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 Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability tRNA mimicry in translation termination and beyond.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.Elongation factor P and modifying enzyme PoxA are necessary for virulence of Shigella flexneri.Biochemistry. Getting past polyproline pauses Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major The bacterial translation stress response.The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Ribosome pausing, arrest and rescue in bacteria and eukaryotes.Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine 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 Arginine-rhamnosylation as new strategy to activate translation elongation factor P Elongation factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence The elongation, termination, and recycling phases of translation in eukaryotes.Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access (R)-β-lysine-modified elongation factor P functions in translation elongation.Nascent peptides that block protein synthesis in bacteria.High-precision analysis of translational pausing by ribosome profiling in bacteria lacking EFP.eIF5A promotes translation of polyproline motifs.Distinct XPPX sequence motifs induce ribosome stalling, which is rescued by the translation elongation factor EF-P 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.Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody.Homocysteine Editing, Thioester Chemistry, Coenzyme A, and the Origin of Coded Peptide Synthesis †.Unique modifications of translation elongation factors.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.Polyamines in Eukaryotes, Bacteria, and Archaea.Identification of an anti-TB compound targeting the tyrosyl-tRNA synthetase.

P2860

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P2860

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

http://www.wikidata.org/entity/Q27664126

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@ast

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@en

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@nl

type

label

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@ast

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@en

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@nl

prefLabel

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@ast

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@en

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@nl

P1433

Q27664126-6848AC89-8782-4DDE-BC40-A266093574EA

P1476

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P2093

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Q27664126-B110AA95-E3F4-4B9F-B32A-DEF8D892B4D3

P2860

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P2888

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P304

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P3181

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P356

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P433

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P577

Q27664126-92F06598-9DC9-4B7C-AD00-61F846A4B92C

P5875

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P6179

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P698

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P921

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P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

A paralog of lysyl-tRNA synthe ...... ranslation elongation factor P

@en

P2093

Chie Takemoto

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

Tatsuo Yanagisawa

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

Tomomi Sumida

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

P2860

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

Crystal structure of elongation factor P from Thermus thermophilus HB8

Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality

Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification

The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)

An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.

P2888

P304

1136-43

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

P31

scholarly article

P3181

1413009

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

P356

10.1038/NSMB.1889

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

P433

9

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

P478

17

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

P50

Shigeyuki Yokoyama

P577

2010-09-01T00:00:00Z

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

P5875

45800279

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

P6179

1011152867

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

P698

20729861

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

P921

bacterial-type EF-P lysine modification

protein-N6-(L-lysyl)-L-lysine modification to protein-N6-(beta-lysyl)-L-lysine

protein-lysine lysylation

protein-lysine lysyltransferase activity