Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit

Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimension...

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Bibliographic Details
Published in:FEBS letters 2005-11, Vol.579 (27), p.6049-6054
Main Authors: Jiang, Shoulei, Wolfe, Cindy L., Warrington, J. Anthony, Norcum, Mona Trempe
Format: Article
Language:English
Subjects:
aa-tRNA
aaRS
aminoacyl-tRNA
Aminoacyl-tRNA synthetase
Antibody
EF-1H
Elongation factor 1
four subunit form of elongation factor 1
Humans
Multiprotein complex
Peptide Elongation Factors - chemistry
Protein biosynthesis
Protein Conformation
Protein Subunits - chemistry
Three-dimensional reconstruction
Valine-tRNA Ligase - chemistry
ValRS
valyl-tRNA synthetase
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Summary:Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis – aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimensional structure of the particle as calculated from electron microscopic images of negatively stained samples of the human ValRS/EF-1H complex. The ca. 12 × 8 nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two δ subunits near the particle’s center. These data support a dimeric head-to-head arrangement of particle components.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2005.09.062