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J Biol Chem, Vol. 274, Issue 14, 9771-9777, April 2, 1999
,,,§
From the The low cytoplasmic and high nuclear
concentration of the GTP-bound form of Ran provides directionality for
both nuclear protein import and export. Both import and export factors
bind RanGTP directly, yet this interaction produces opposite effects;
in the former case, RanGTP binding induces nuclear cargo release,
whereas in the latter, RanGTP binding induces nuclear cargo assembly. Therefore, nuclear import and export receptors and their protein recognition sites are predicted to be distinct. Nevertheless, the
~38-amino acid M9 sequence present in heterogeneous nuclear ribonucleoprotein A1 has been reported to serve as both a nuclear localization signal and a nuclear export signal, even though only one
protein, the nuclear import factor transportin, has been shown to bind
M9 directly. We have used a combination of mutational randomization
followed by selection for transportin binding to exhaustively define
amino acids in M9 that are critical for transportin binding in
vivo. As expected, the resultant ~12-amino acid
transportin-binding consensus sequence is also predictive of nuclear
localization signal activity. Surprisingly, however, this extensive
mutational analysis failed to dissect M9 nuclear localization signal
and nuclear export signal function. Nevertheless, transportin appears unlikely to be the M9 export receptor, as RanGTP can be shown to block
M9 binding by transportin not only in vitro, but also in
the nucleus in vivo. This analysis therefore predicts the
existence of a nuclear export receptor distinct from transportin that
nevertheless shares a common protein-binding site on heterogeneous
nuclear ribonucleoprotein A1.
Howard Hughes Medical Institute and the
§ Department of Genetics, Duke University Medical Center,
Durham, North Carolina 27710
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