Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents.  Importance of hydrophobic interactions and possible involvement of lipids. 
In order to gain some insight into the structural parameters important for aminoacyl-tRNA synthetase complex formation, we have examined the effect of various salts and detergents on the stability and structure of the synthetase complex.  Certain neutral salts were found to inactivate aminoacyl-tRNA synthetase activities in the complex, and the order of effectiveness in this process followed a classical Hofmeister series.  In addition, one of these salts, NaSCN, was also effective in partially dissociating the complex.  Detergents varied in their ability to inactivate synthetases, with ionic detergents being most effective and nonionic detergents being much less destructive.  Detergents, by themselves, could partially disrupt the complex; however, in the presence of 1 M NaCl, nonionic detergents did lead to considerable dissociation of synthetases and generation of low molecular weight forms of these enzymes.  Removal of lipids from the complex with the nonionic detergent, Triton X-114, rendered arginyl-tRNA synthetase sensitive to the addition of NaCl.  However, this salt sensitivity was abolished by readdition of a lipid extract isolated from the complex.  These results implicate hydrophobic interactions in the stability of the synthetase complex, and suggest the possible involvement of lipids in maintaining its structural integrity.