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Papers In Press, published online ahead of print August 4, 2000
Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33101-6129
Corresponding Author: mdeutsch{at}med.miami.edu
Recent studies suggest that aminoacylation of tRNA may play an important role in the transport of these molecules from the nucleus to the cytoplasm. However, there is almost no information regarding the status of active aminoacyl-tRNA synthetases within the nuclei of eukaryotic cells. Here we show that at least thirteen active aminoacyl-tRNA synthetases are present in purified nuclei of both CHO and rabbit kidney cells, although their steady-state levels represent only a small percentage of those found in the cytoplasm. Most interestingly, all the nuclear aminoacyl-tRNA synthetases examined can be isolated as part of a multienzyme complex that is more stable, and consequently larger, than the comparable complex isolated from the cytoplasm. These data directly demonstrate the presence of active aminoacyl-tRNA synthetases in mammalian cell nuclei. Moreover, their unexpected structural organization raises important questions about the functional significance of these multienzyme complexes and whether they might play a more direct role in nuclear to cytoplasmic transport of tRNAs.
J. Biol. Chem, 10.1074/jbc.C000385200
Submitted on June 15, 2000
Revised on August 3, 2000
Accepted on August 4, 2000
Active Aminoacyl-tRNA Synthetases are Present in Nuclei as a High Molecular Weight Multienzyme Complex
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