Faculty Opinions recommendation of A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation 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.

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

FEBS Letters ◽

10.1016/0014-5793(96)00128-7 ◽

1996 ◽

Vol 382 (1-2) ◽

pp. 18-20 ◽

Cited By ~ 24

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

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

Acta Crystallographica Section F Structural Biology and Crystallization Communications ◽

10.1107/s1744309110032008 ◽

2010 ◽

Vol 66 (9) ◽

pp. 1115-1118 ◽

Cited By ~ 2

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.

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