Hierarchical network between the components of the multi-tRNA synthetase complex: implications for complex formation.
The macromolecular tRNA synthetase complex consists of nine different enzymes and three non-enzymatic factors. This complex was recently shown to be a novel signalosome, since many of its components are involved in signaling pathways in addition to their catalytic roles in protein synthesis. The structural organization and dynamic relationships of the components of the complex are not well understood. Here we performed a systematic depletion analysis to determine the effects of structural intimacy and the turnover of the components. The results showed that the stability of some components depended on their neighbors. Lysyl-tRNA synthetase was most independent of other components for its stability whereas it was most required for the stability of other components. Arginyl- and methionyl-tRNA synthetases had the opposite characteristics. Thus, the systematic depletion of the components revealed the functional reason for the complex formation and the assembly pattern of these multi-functional enzymes and their associated factors.
Han
Jung Min
JM
Imagene Company Biotechnology Incubating Center, Golden Helix, Seoul National University, Seoul 151-741, Korea.
Lee
Min Ji
MJ
Park
Sang Gyu
SG
Lee
Sun Hee
SH
Razin
Ehud
E
Choi
Eung-Chil
EC
Kim
Sunghoon
S
D000604:Amino Acyl-tRNA Synthetases / Q000096:biosynthesis / Q000378:metabolism*; D001483:Base Sequence; D002850:Chromatography, Gel; D006367:HeLa Cells; D006801:Humans; D034741:RNA, Small Interfering; D020133:Reverse Transcriptase Polymerase Chain Reaction
D034741:RNA, Small Interfering; D000604:Amino Acyl-tRNA Synthetases