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J Biol Chem, Vol. 274, Issue 41, 29031-29037, October 8, 1999
From the Department of Cell Biology, University of Alberta,
Edmonton, Alberta T6G 2H7, Canada
Kap104p is a Saccharomyces cerevisiae
nuclear import receptor for two essential mRNA-binding proteins,
Nab2p and Nab4p/Hrp1p. We demonstrate direct binding of Kap104p to each
of these substrates. We have defined the nuclear localization signals
in both Nab2p and Nab4p/Hrp1p by Kap104p binding in vitro
and KAP104-dependent nuclear import in
vivo. The nuclear localization signals map to similar
arginine/glycine-rich RNA-binding domains in both proteins and are thus
termed rg-nuclear localization signals to distinguish them from
classical nuclear localization signals. We also demonstrate that
Kap104p, like other known
Kap104p-mediated Nuclear Import
NUCLEAR LOCALIZATION SIGNALS IN mRNA-BINDING PROTEINS AND
THE ROLE OF RAN AND RNA
-karyopherins (or importins), interacts
directly with the small GTPase Ran/Gsp1. However, unlike other known
import factors, Ran binding is not sufficient to mediate release of
substrates from Kap104p; efficient Ran-GTP-mediated substrate release
requires RNA. Also, addition of Kap104p to Nab2p and Nab4p/Hrp1p
prebound to single-stranded DNA-cellulose stimulated release of both
proteins from the resin. We suggest a simple cycle in which Nab2p and
Nab4p/Hrp1p, upon import, are released in the nucleus at sites of
transcription by the concerted action of Ran-GTP and binding to newly
synthesized mRNA. The resulting ribonucleoprotein complexes are
exported to the cytoplasm, where Kap104p rebinds to Nab2p and
Nab4p/Hrp1p, contributing to their release from mRNA.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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