The high molecular weight aminoacyl-tRNA synthetase complexes found in extracts of many eukaryotic cells often contain lipids and other non-protein components. Since hydrophobic interactions play an important role in maintaining synthetases in the complex, it has been suggested that the lipids present may also participate in its functional and structural integrity. In order to learn more about the role of lipids in the complex, we have compared the properties of the normal complex to one which has been delipidated by treatment with Triton X-114. Delipidation does not affect the size or activity of the aminoacyl-tRNA synthetase complex, but a variety of functional and structural properties of individual synthetases in the complex are altered dramatically. These include sensitivity to salts plus detergents, temperature inactivation, hydrophobicity, and sensitivity to protease digestion. In the latter case, removal of lipids also affects the low molecular weight products released by protease digestion. Purification of the synthetase complex by various chromatographic procedures can remove the lipids and lead to a structure that behaves like the delipidated complex prepared by detergent treatment. The significance of these findings for the intracellular location of aminoacyl-tRNA synthetases and for the study of purified complexes are discussed.
|Original language||English (US)|
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|State||Published - Dec 1 1988|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology