Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro.
The functions of evolved mammalian supramolecular assemblies and extensions of enzymes are not well understood. Human lysyl-tRNA synthetase (hKRS) only upon the removal of the amino-terminal extension (hKRSDelta60) bound to EF1alpha and was stimulated by EF1alphain vitro. HKRS and hKRSDelta60 were also differentially stimulated by aspartyl-tRNA synthetase (AspRS) from the multi-synthetase complex. The non-synthetase protein from the multi-synthetase complex p38 alone did not affect hKRS lysylation but inhibited the AspRS-mediated stimulation of hKRS. These results revealed the functional interactions of hKRS and shed new lights on the functional significance of the structural evolution of multienzyme complexes and appended extensions.
Guzzo
Catherine M
CM
Department of Chemistry, Georgetown University, Washington, DC 20057, USA.
Yang
David C H
DC
D008250:Lysine-tRNA Ligase / Q000378:metabolism*; D020648:Peptide Elongation Factor 1 / Q000378:metabolism*; D025941:Protein Interaction Mapping; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D020798:Two-Hybrid System Techniques; D048051:p38 Mitogen-Activated Protein Kinases / Q000378:metabolism*
D020648:Peptide Elongation Factor 1; D012346:RNA, Transfer, Amino Acyl; D048051:p38 Mitogen-Activated Protein Kinases; D008250:Lysine-tRNA Ligase