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A more recent version of this article appeared on January 1, 2004
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Submitted on June 17, 2003
Revised on September 8, 2003
Accepted on September 22, 2003
1 Interdepartmental Program in Cell and Molecular Biology, Dept. of Molecular and Cellular Biology; Baylor College of Medicine, One Baylor Plaza, Houston, TX. 77030; These two authors contributed equally to this work
2 Dept. of Molecular and Cellular Biology; Baylor College of Medicine, One Baylor Plaza, Houston, TX. 77030; These two authors contributed equally to this work
3 Interdepartmental Program in Cell and Molecular Biology, Dept. of Molecular and Cellular Biology; Baylor College of Medicine, One Baylor Plaza, Houston, TX. 77030
* Corresponding author. E-mail address: mmoore{at}bcm.tmc.edu.
RCC1 binding to chromatin is highly dynamic, as determined by FRAP
analysis of GFP-RCC1 in stably transfected tsBN2 cells. Microinjection
of wt or Q69L Ran markedly slowed the mobility of GFP-RCC1, while T24N
Ran (defective in nucleotide loading) decreased it further still. We
found significant alterations in the mobility of intranuclear GFP-RCC1
after treatment with agents that disrupt different Ran-dependent
nuclear export pathways. Leptomycin B, which inhibits
Crm1/RanGTP-dependent nuclear export, significantly increased the
mobility of RCC1 as did high levels of actinomycin D (to inhibit RNA
polymerases I, II, and III) or 
-amanitin (to inhibit RNA
polymerases II and III) as well as energy depletion. Inhibition of just
mRNA transcription, however, had no affect on GFP-RCC1 mobility
consistent with mRNA export being a Ran-independent process. In
permeabilized cells, cytosol and GTP were required for the efficient
release of GFP-RCC1 from chromatin. Recombinant Ran would not
substitute for cytosol, and high levels of supplemental Ran inhibited
the cytosol-stimulated release. Thus, RCC1 release from chromatin in
vitro requires a factor(s) distinct from, or in addition to, Ran and
appears linked in vivo to the availability of Ran-dependent transport
cargo.
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