High impact information on Lars

• Regulation of polypeptide chain initiation in Chinese hamster ovary cells with a temperature-sensitive leucyl-tRNA synthetase. Changes in phosphorylation of initiation factor eIF-2 and in the activity of the guanine nucleotide exchange factor GEF [1].
• Characterization of cell lines showing growth control isolated from both the wild type and a leucyl-tRNA synthetase mutant of Chinese hamster ovary cells [2].
• The CHO cell line has yielded many recessive mutations including, for example, tsH1, a temperature sensitive leucyl-tRNA synthetase mutant, which under non-permissive conditions rapidly shuts down protein synthesis and generates uncharged tRNA [2].
• CONCLUSIONS: Cadmium ions significantly reduce activities of tRNA(Leu)and leucyl-tRNA synthetase in vivo and in vitro [3].
• Acceptor activity of tRNA(Leu)and activity of leucyl-tRNA synthetase were measured in tRNA aminoacylation reaction with [14C]-labeled leucine as a substrate [3].

Biological context of Lars

• Since the primary lesion in tsH1 cells is in their leucyl-tRNA synthetase, these results suggest a role for eIF-2 phosphorylation and GEF activity in coupling the rate of polypeptide chain initiation to the activity of the chain elongation machinery [1].

Anatomical context of Lars

• Post-mitochondrial fraction of the liver cells was used as a source of leucyl-tRNA synthetase [3].

Other interactions of Lars

• Analysis of the size-distribution of partially purified leucyl-tRNA synthetase complexes indicated that, while enzyme preparations from young animals tended to consist of complexes of larger sizes, those from older animals contained smaller complexes, a 10S complex being a major component [4].

References