EC Number   |
General Information |
Reference |
|---|
    6.1.1.9 | evolution |
glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase |
745020 |
| 6.1.1.9 | evolution |
the enzyme belongs to the class I aminoacyl-tRNA synthetases |
744977 |
| 6.1.1.9 | evolution |
the proline triplet in ValS, the tRNA synthetase that charges tRNAVal with valine, is the only single polyproline stretch that is invariant across all domains of life. The critical role of the proline triplet for ValS activity may explain why bacterial cells co-evolved the EF-P rescue system. Nature has evolved not only specialized translation factors to overcome stalling at polyproline stretches, but also evolved independent sets of modification enzymes to activate these factors. This in itself implies that the benefits of retaining polyproline stretches significantly outweigh the cost of implementing and maintaining the EF-P and a/eIF5A rescue systems |
744659 |
| 6.1.1.9 | malfunction |
a single base change in OsValRS2 causes virescent to albino mutant phenotypes in seedlings and white panicles at heading, termed the white panicle 1 (wp1) mutant. The white panicle1 mutant form of a Val-tRNA synthetase from Oryza sativa is targeted to both chloroplasts and mitochondria. The wp1 mutants are defective in early chloroplast development, and wp1 is impaired in chloroplast ribosome biogenesis. Expression of nuclear-encoded photosynthetic genes is significantly repressed, while expression of many chloroplast-encoded genes also changed significantly in wp1 mutants, although mRNA levels of some genes are higher in wp1 than in wild-type. Phenotype, overview |
746112 |
| 6.1.1.9 | more |
analysis of aminoacyl-tRNA synthetases protein interactions, overview. The Anabaena sp. ValRs is a CAAD-containing aaRSs, the CAAD domain possesses an inherent membrane targeting ability |
744977 |
| 6.1.1.9 | more |
expression of ValS is strictly dependent on the presence of active elongation factor P (EF-P) in vivo and in vitro |
744659 |
| 6.1.1.9 | more |
human valyl-tRNA synthetase and mitochondrial protein elongation factor EF-Tu show suppressing cross-activity on different tRNA mutants in humans and Saccharomyces cerevisiae, mechanism and specificity of suppression, overview. Suppressive activities of wild-type and mutant enzymes, overview |
714322 |
| 6.1.1.9 | more |
molecular trigger for pre-transfer editing pathway in valyl-tRNA synthetase, molecular dynamics simulations using ValRS structure, PDB ID 1GAX, overview. Structural models of the complexes ValRS-tRNAval-Val-AMP and ValRS-tRNAval-Thr-AMP |
715972 |
| 6.1.1.9 | more |
structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate |
745020 |
| 6.1.1.9 | physiological function |
gene is active and essential for the survival of the yeast |
705623 |
