L. Nathanson et Mp. Deutscher, Accelerated publication - Active aminoacyl-tRNA synthetases are present innuclei as a high molecular weight multienzyme complex, J BIOL CHEM, 275(41), 2000, pp. 31559-31562
Recent studies suggest that aminoacylation of tRNA may play an important ro
le in the transport of these molecules from the nucleus to the cytoplasm. H
owever, there is almost no information regarding the status of active amino
acyl-tRNA synthetases within the nuclei of eukaryotic cells. Here we show t
hat at least 13 active aminoacyl-tRNA synthetases are present in purified n
uclei of both Chinese hamster ovary and rabbit kidney cells, although their
steady-state levels represent only a small percentage of those found in th
e cytoplasm. Most interestingly, all the nuclear aminoacyl-tRNA synthetases
examined can be isolated as part of a multienzyme complex that is more sta
ble, and consequently larger, than the comparable complex isolated from the
cytoplasm. These data directly demonstrate the presence of active aminoacy
l-tRNA synthetases in mammalian cell nuclei. Moreover, their unexpected str
uctural organization raises important questions about the functional signif
icance of these multienzyme complexes and whether they might play a more di
rect role in nuclear to cytoplasmic transport of tRNAs.