Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit
Abstract
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.
- Publication:
-
FEBS Letters
- Pub Date:
- January 2005
- DOI:
- 10.1016/j.febslet.2005.09.062
- Bibcode:
- 2005FEBSL.579.6049J
- Keywords:
-
- aaRS;
- aminoacyl-tRNA synthetase;
- ValRS;
- valyl-tRNA synthetase;
- EF-1H;
- four subunit form of elongation factor 1;
- aa-tRNA;
- aminoacyl-tRNA;
- Aminoacyl-tRNA synthetase;
- Elongation factor 1;
- Three-dimensional reconstruction;
- Protein biosynthesis;
- Multiprotein complex;
- Antibody