Nucleic Acids Research, Vol 27, Issue 21 4128-4134, Copyright © 1999 by Oxford University Press
U Fischer, VW Pollard, R Luhrmann, M Teufel, MW Michael, G Dreyfuss and MH Malim
The human immunodeficiency virus type-1 Rev protein induces the nuclear
export of intron-containing viral mRNAs that harbor its binding site, the
Rev response element (RRE). A leucine-rich region of Rev, the activation
domain, is essential for function and has been shown to be a nuclear export
signal (NES). Although Rev exports viral RNAs that resemble cellular mRNAs,
competition studies performed using microinjected Xenopus laevis oocytes
have previously indicated that Rev utilizes a non-mRNA export pathway.
Here, we show that Rev is able to induce the export of both spliceable and
non-spliceable RRE-containing pre-mRNAs and that this activity is not
dependent on the location of the RRE within the RNA. Importantly, even RNA
molecules of different classes, such as U3 snoRNA and U6 snRNA, which are
retained in the nucleus by non-pre-mRNA mechanisms, are exported to the
cytoplasm in response to Rev. Consistent with the notion that Rev-mediated
export of RRE-containing RNA is mechanistically distinct from the export of
processed cellular mRNA, a chimeric Rev protein in which its NES is
replaced by the NES of hnRNP A1 does not induce the export of a Rev-
responsive mRNA. Finally, we demonstrate that Rev/RRE-activated RNA export
is, like other nuclear export pathways, linked to the Ran-GTPase cycle.
ARTICLES
Rev-mediated nuclear export of RNA is dominant over nuclear retention and is coupled to the Ran-GTPase cycle
Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany. ufischer@biochem.mpg.de
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