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

2010 ◽  
Vol 17 (9) ◽  
pp. 1136-1143 ◽  
Author(s):  
Tatsuo Yanagisawa ◽  
Tomomi Sumida ◽  
Ryohei Ishii ◽  
Chie Takemoto ◽  
Shigeyuki Yokoyama
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Lysine Residue ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Elongation Factor P

scholarly journals Arginine-rhamnosylation as new strategy to activate translation elongation factor P

2015 ◽  
Vol 11 (4) ◽  
pp. 266-270 ◽  
Author(s):  
Jürgen Lassak ◽  
Eva C Keilhauer ◽  
Maximilian Fürst ◽  
Kristin Wuichet ◽  
Julia Gödeke ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
New Strategy ◽  
Elongation Factor P

scholarly journals Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl-tRNA synthetase

2002 ◽  
Vol 269 (19) ◽  
pp. 4811-4818 ◽  
Author(s):  
Zoya M. Petrushenko ◽  
Tatyana V. Budkevich ◽  
Vyacheslav F. Shalak ◽  
Boris S. Negrutskii ◽  
Anna V. El'skaya
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Translation Elongation Factor ◽  
Translation Elongation

scholarly journals Erratum: Corrigendum: Arginine-rhamnosylation as new strategy to activate translation elongation factor P

2015 ◽  
Vol 11 (4) ◽  
pp. 299-299 ◽  
Author(s):  
Jürgen Lassak ◽  
Eva C Keilhauer ◽  
Maximilian Fürst ◽  
Kristin Wuichet ◽  
Julia Gödeke ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
New Strategy ◽  
Elongation Factor P

scholarly journals Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability

PLoS ONE ◽  
2016 ◽  
Vol 11 (2) ◽  
pp. e0147907 ◽  
Author(s):  
Tatsuo Yanagisawa ◽  
Hideyuki Takahashi ◽  
Takehiro Suzuki ◽  
Akiko Masuda ◽  
Naoshi Dohmae ◽  
...  
Keyword(s):  
Cell Viability ◽  
Neisseria Meningitidis ◽  
Active Site ◽  
Elongation Factor ◽  
Arginine Residue ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Elongation Factor P

scholarly journals Translation elongation factor P (EF-P)

2020 ◽  
Vol 44 (2) ◽  
pp. 208-218 ◽  
Author(s):  
Katherine R Hummels ◽  
Daniel B Kearns
Keyword(s):  
Elongation Factor ◽  
Peptide Bond ◽  
Post Translational Modification ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Isolation And Characterization ◽  
Domains Of Life ◽  
Ribosome Pausing ◽  
Elongation Factor P

ABSTRACT Translation elongation factor P (EF-P) is conserved in all three domains of life (called eIF5A and aIF5A in eukaryotes and archaea, respectively) and functions to alleviate ribosome pausing during the translation of specific sequences, including consecutive proline residues. EF-P was identified in 1975 as a factor that stimulated the peptidyltransferase reaction in vitro but its involvement in the translation of tandem proline residues was not uncovered until 2013. Throughout the four decades of EF-P research, perceptions of EF-P function have changed dramatically. In particular, while EF-P was thought to potentiate the formation of the first peptide bond in a protein, it is now broadly accepted to act throughout translation elongation. Further, EF-P was initially reported to be essential, but recent work has shown that the requirement of EF-P for growth is conditional. Finally, it is thought that post-translational modification of EF-P is strictly required for its function but recent studies suggest that EF-P modification may play a more nuanced role in EF-P activity. Here, we review the history of EF-P research, with an emphasis on its initial isolation and characterization as well as the discoveries that altered our perceptions of its function.

scholarly journals Rabbit translation elongation factor 1α stimulates the activity of homologous aminoacyl-tRNA synthetase

FEBS Letters ◽  
1996 ◽  
Vol 382 (1-2) ◽  
pp. 18-20 ◽  
Author(s):  
Boris S Negrutskii ◽  
Tatyana V Budkevich ◽  
Vyacheslav F Shalak ◽  
Galina V Turkovskaya ◽  
Anna V El'Skaya
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Translation Elongation Factor ◽  
Elongation Factor 1Α ◽  
Translation Elongation ◽  
Translation Elongation Factor 1Α

scholarly journals Crystallization and preliminary X-ray crystallographic study of GenX, a lysyl-tRNA synthetase paralogue fromEscherichia coli, in complex with translation elongation factor P

2010 ◽  
Vol 66 (9) ◽  
pp. 1115-1118 ◽  
Author(s):  
Tomomi Sumida ◽  
Tatsuo Yanagisawa ◽  
Ryohei Ishii ◽  
Shigeyuki Yokoyama
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Unit Cell ◽  
Translation Elongation Factor ◽  
Unit Cell Parameters ◽  
Translation Elongation ◽  
Space Group ◽  
Cell Parameters ◽  
E Coli ◽  
Peg 4000

GenX, a lysyl-tRNA synthetase paralogue fromEscherichia coli, was overexpressed inE. coli, purified by three chromatographic steps and cocrystallized with a lysyl adenylate analogue (LysAMS) by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The GenX–LysAMS crystals belonged to the triclinic space groupP1, with unit-cell parametersa = 54.80,b= 69.15,c = 94.08 Å, α = 95.47, β = 106.51, γ = 90.46°, and diffracted to 1.9 Å resolution. Furthermore, GenX was cocrystallized with translation elongation factor P (EF-P), which is believed to be a putative substrate of GenX, and LysAMS using PEG 4000 and ammonium sulfate as precipitants. The GenX–EF-P–LysAMS crystals belonged to the monoclinic space groupP21, with unit-cell parametersa = 105.93,b= 102.96,c= 119.94 Å, β = 99.4°, and diffracted to 2.5 Å resolution. Structure determination of theE. coliGenX–LysAMS and GenX–EF-P–LysAMS complexes by molecular replacement was successful and structure refinements are now in progress.

scholarly journals Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody

2016 ◽  
Vol 7 (12) ◽  
pp. 6995-7001 ◽  
Author(s):  
Xiang Li ◽  
Ralph Krafczyk ◽  
Jakub Macošek ◽  
Yu-Lei Li ◽  
Yan Zou ◽  
...  
Keyword(s):  
Specific Antibody ◽  
Elongation Factor ◽  
Glycosidic Linkage ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Novel Antibiotics ◽  
Elongation Factor P

Here we describe a potent tool to investigate arginine rhamnosylation and develop novel antibiotics.

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