Glutaminyl-tRNA synthetase as a component of the high-molecular weight complex of human aminoacyl-tRNA synthetases. An immunological study.
The human glutaminyl-tRNA synthetase is three times larger than the corresponding bacterial and twice as large as the yeast enzyme. It is possible that the additional sequences of the human glutaminyl-tRNA synthetase are required for the formation of the multienzyme complex which is known to include several of aminoacyl-tRNA synthetases in mammalian cells. To address this point we prepared antibodies against three regions of the human glutaminyl-tRNA synthetase, namely against its enzymatically important core region, and against two sections in its large C-terminal extension. In intact multienzyme complexes the core region was accessible to specific antibody binding. However, the C-terminal sections became available to specific antibody binding only when certain components of the multienzyme complex were either absent or degraded. These findings allow first conclusions as to the relative position of some components in the mammalian aminoacyl-tRNA synthetase complex.
Schray
B
B
Fakultät für Biologie, Universität Konstanz, F.R.G.
Thömmes
P
P
Knippers
R
R
D000604:Amino Acyl-tRNA Synthetases / Q000276:immunology / Q000378:metabolism*; D000918:Antibody Specificity; D002478:Cells, Cultured; D002498:Centrifugation; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D008970:Molecular Weight; D009097:Multienzyme Complexes; D011233:Precipitin Tests
D009097:Multienzyme Complexes; D000604:Amino Acyl-tRNA Synthetases; C020659:glutaminyl-tRNA synthetase