Aminoacyl-Transfer RNA Synthetases

Mitochondrial-specific aminoacyl-RNA synthetases.

Numerous lines of evidencel'indicate that protein synthesis occurs within mitochondria, and tRNA8, 15, 16 and aminoacyl-RNA synthetases8 have been prepared from these organelles. More recently, two very interesting aspects of mitochondrial protein synthesis have been described: (a) Although amino acid incorporation by yeast cytoplasmic ribosomal systems is not inhibited by chloramphenicol,'7 pr...

Differences between mitochondrial and cytoplasmic transfer RNA and aminoacyl transfer RNA synthetases from rat liver.

The mitochondria of yeast,1 Neurospora,2 and Tetrahymena3 have been shown to contain transfer RNA (tRNA). Barnett et al.4 have found, in addition, that Neurospora mitochondria contain 15 aminoacyl-tRNA synthetases, at least three of which acylate only mitochondrial tRNA. The purpose of this communication is twofold. First we will present evidence showing that, as with eukaryotic microbial syste...

More evidence for a particle character of aminoacyl-transfer RNA synthetases isolated from rat liver.

Aminoacyl-tRNA synthetases database

Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the firs...

RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes.

Here, we examine tRNA-aminoacyl synthetase (ARS) localization in protein synthesis. Proteomics reveals that ten of the twenty cytosolic ARSs associate with ribosomes in sucrose gradients: phenylalanyl-RS (FRS), and the 9 ARSs that form the multi-ARS complex (MSC). Using the ribopuromycylation method (RPM) for localizing intracellular translation, we show that FRS and the MSC, and to a lesser ex...