Bovine tryptophanyl-tRNA synthetase and glyceraldehyde-3-phosphate dehydrogenase form a complex.
Bovine tryptophanyl-tRNA synthetase is able to form a complex with glyceraldehyde-3-phosphate dehydrogenase. The complex formation (i) does not influence the tryptophan-dependent PPi-ATP exchange reaction and (ii) involves predominantly the N-terminal dispensable domain of the synthetase. Glyceraldehyde-3-phosphate dehydrogenase was shown to be capable of interacting simultaneously with tryptophanyl-tRNA synthetase and with ribosomal RNA to form a ternary complex. It is proposed that compartmentation of some aminoacyl-tRNA synthetases in certain cases might be achieved via 'adapter' molecules which can bind at once to ribonucleic acids and to aminoacyl-tRNA synthetases.
Filonenko
V V
VV
Engelhardt Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Beresten
S F
SF
Rubikaite
B I
BI
Kisselev
L L
LL
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002451:Cell Compartmentation; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D009097:Multienzyme Complexes; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism; D014369:Tryptophan-tRNA Ligase / Q000378:metabolism*
D009097:Multienzyme Complexes; D012335:RNA, Ribosomal; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D000604:Amino Acyl-tRNA Synthetases; D014369:Tryptophan-tRNA Ligase