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Volume 270,
Number 18,
Issue of May 5, pp. 10658-10663, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
The RCC1 Protein
Interacts with Ran, RanBP1, hsc70, and a 340-kDa Protein in
Xenopus Extracts
Hisato
Saitoh
,
Mary
Dasso
RCC1 is an abundant, highly conserved, chromatin-associated
protein whose function is necessary for the preservation of a properly
ordered cell cycle. RCC1 is also necessary for numerous nuclear
processes, including nuclear transport and RNA metabolism; and it
functions enzymatically as a guanine nucleotide exchange factor for a
small, ras-related GTPase called Ran. Studies in several
organisms suggest that RCC1 may be part of a large complex containing
multiple proteins. There is also evidence that RCC1 associates with
chromatin through other proteins and that the binding of the complex to
chromatin varies within the cell cycle. In order to characterize this
putative complex, we have identified a number of other proteins as
candidate components of the complex by their association with a
GST-RCC1 fusion protein. Three of these proteins have previously been
identified (Ran, RanBP1, and hsc70). The fourth protein is novel and
has a molecular mass of 340 kDa. In this report, we discuss a
preliminary characterization of the interactions between these
proteins.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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