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Abstract 


The mechanism by which a tRNA molecule is delivered from the nucleus of a cell to the cytoplasm has been studied in the Xenopus laevis oocyte utilizing nuclear microinjection and manual microdissection techniques. tRNA nuclear transport in this cell resembles a carrier-mediated translocation process rather than diffusion through a simple pore or channel. tRNA transport is saturable by tRNA, with a maximal rate measured to be about 190 X 10(7) molecules per min per nucleus (21 degrees C) in the mature oocyte. Competitive inhibition between two different tRNA species can be demonstrated, suggesting that many tRNA species share a common carrier system. tRNA nuclear transport is sharply dependent on temperature, with an optimal rate observed at 31 degrees C. A single G-to-U substitution at position 57 in the vertebrate tRNAMeti molecule reduces the transport rate of this tRNA by a factor of about 20, implicating this highly conserved region of the tRNA molecule (loop IV) as critical for recognition by the transport mechanism. On morphologic grounds I propose that ribosome-like components surrounding the nuclear pore may function as the tRNA translocation "motor." The tRNA nuclear transport mechanism represents a distinctly eukaryotic process and a site of potential control over cell growth and proliferation.

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Proc Natl Acad Sci U S A. 1983 Nov; 80(21): 6436–6440.
PMCID: PMC390128
PMID: 6579529

tRNA transport from the nucleus in a eukaryotic cell: carrier-mediated translocation process.

Abstract

The mechanism by which a tRNA molecule is delivered from the nucleus of a cell to the cytoplasm has been studied in the Xenopus laevis oocyte utilizing nuclear microinjection and manual microdissection techniques. tRNA nuclear transport in this cell resembles a carrier-mediated translocation process rather than diffusion through a simple pore or channel. tRNA transport is saturable by tRNA, with a maximal rate measured to be about 190 X 10(7) molecules per min per nucleus (21 degrees C) in the mature oocyte. Competitive inhibition between two different tRNA species can be demonstrated, suggesting that many tRNA species share a common carrier system. tRNA nuclear transport is sharply dependent on temperature, with an optimal rate observed at 31 degrees C. A single G-to-U substitution at position 57 in the vertebrate tRNAMeti molecule reduces the transport rate of this tRNA by a factor of about 20, implicating this highly conserved region of the tRNA molecule (loop IV) as critical for recognition by the transport mechanism. On morphologic grounds I propose that ribosome-like components surrounding the nuclear pore may function as the tRNA translocation "motor." The tRNA nuclear transport mechanism represents a distinctly eukaryotic process and a site of potential control over cell growth and proliferation.

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Selected References

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