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Published 19 December 2005. doi:10.1083/jcb.200509061
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 6, 955-965
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Article

 The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in endogenous NPC-mediated transcriptional control

David J. Dilworth1,2, Alan J. Tackett3, Richard S. Rogers1, Eugene C. Yi1, Rowan H. Christmas1, Jennifer J. Smith1, Andrew F. Siegel1,4, Brian T. Chait3, Richard W. Wozniak2, and John D. Aitchison1,2

1 Institute for Systems Biology, Seattle, WA 98103
2 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
3 The Rockefeller University, New York, NY 10021
4 Departments of Management Science, Finance, and Statistics, The University of Washington, Seattle, WA 98195

Correspondence to John Aitchison: jaitchison{at}systemsbiology.org

Nuclear pore complexes (NPCs) govern macromolecular transport between the nucleus and cytoplasm and serve as key positional markers within the nucleus. Several protein components of yeast NPCs have been implicated in the epigenetic control of gene expression. Among these, Nup2p is unique as it transiently associates with NPCs and, when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity. To understand this function of Nup2p, we investigated the interactions of Nup2p with other proteins and with DNA using immunopurifications coupled with mass spectrometry and microarray analyses. These data combined with functional assays of boundary activity and epigenetic variegation suggest that Nup2p and the Ran guanylyl-nucleotide exchange factor, Prp20p, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization by facilitating the transition of chromatin between activity states.

Abbreviations used in this paper: BA, boundary activity; ChIP-CHIP, chromatin immunopurification microarray; Gbd, Gal4p DNA binding domain; NE, nuclear envelope; NPC, nuclear pore complex; Nup, nucleoporin; prA, protein A.


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