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Title
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RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiae.
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Authors
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J.Becker,
F.Melchior,
V.Gerke,
F.R.Bischoff,
H.Ponstingl,
A.Wittinghofer.
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Ref.
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J Biol Chem, 1995,
270,
11860-11865.
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PubMed id
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Abstract
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Ran/TC4 is a ras-related GTP-binding protein predominantly located in the
nucleus. Ran/TC4 is essential for nuclear transport and is involved in mitotic
control. In Saccharomyces cerevisiae a gene highly homologous to Ran/TC4 has
been identified and named GSP1. Like all ras-related GTP-binding proteins, Gsp1p
undergoes cycles of GTP hydrolysis and GDP/GTP exchange. The switching between
the two different nucleotide bound states regulates the function of these
GTP-binding proteins. Here we identify the product of the yeast RNA1 gene as the
GTPase-activating protein (GAP) of Gsp1p. RNA1 belongs to a group of genes which
are conserved in a variety of different organisms. We have expressed and
purified recombinant Gsp1p and Rna1p from Escherichia coli. The GTPase activity
of Gsp1p is stimulated 10(7)-fold by Rna1p. In addition, we find that the
previously identified human RanGAP1 and rna1p from Schizosaccharomyces pombe are
also able to induce GTPase activity of Gsp1p. The GTP hydrolysis of Ran is
induced by RanGAP1 and rna1p but not by Rna1p. Implications for the suggested
functions of Ran/TC4/Gsp1p in nuclear transport and mitotic control are
discussed.
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