A Root-Specific Iron-Regulated Gene of Tomato Encodes a Lysyl-tRNA-Synthetase-Like Protein

Lysyl-tRNA synthetase gene of Campylobacter jejuni.

We report the cloning and complete nucleotide sequence of the Campylobacter jejuni lysyl-tRNA synthetase gene (lysS). The C. jejuni lysS gene sequence shows high homology to the two Escherichia coli lysyl-tRNA synthetase genes, lysS and lysU. The Campylobacter lysyl-tRNA synthetase protein (LysRS) shows 47.9 and 46.6% sequence identity to the E. coli enzymes encoded by the lysS and lysU genes, ...

Specific Inhibition of the Synthesis of Human Lysyl-tRNA Synthetase

Viral hijacking of mitochondrial lysyl-tRNA synthetase.

The primer for reverse transcription of the human immunodeficiency virus type 1 (HIV-1) genome is tRNA3(Lys). During assembly of HIV-1 particles, tRNA3(Lys) is taken up from the host cell along with lysyl-tRNA synthetase (LysRS), the tRNA binding protein that specifically aminoacylates the different tRNA(Lys) isoacceptors. In humans, the cytoplasmic and mitochondrial species of LysRS are encode...

Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli.

The lysU gene encoding lysyl-tRNA synthetase of Escherichia coli is normally silent at low temperatures and is expressed by certain metabolites and stimuli. A novel class of lysU-constitutive mutations were isolated by random insertion mutagenesis. These mutations nullified the hns gene encoding a histone-like protein, H-NS, and affected thermoregulation of lysU.

Functional dissection of the eukaryotic-specific tRNA-interacting factor of lysyl-tRNA synthetase.

In the cytoplasm of higher eukaryotic cells, aminoacyl-tRNA synthetases (aaRSs) have polypeptide chain extensions appended to conventional prokaryotic-like synthetase domains. The supplementary domains, referred to as tRNA-interacting factors (tIFs), provide the core synthetases with potent tRNA-binding capacities, a functional requirement related to the low concentration of free tRNA prevailin...