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Event

Biochemistry Seminar Dr. Richard Wozniak

Friday, May 14, 2010 13:00
McIntyre Medical Building 3655 promenade Sir William Osler, Montreal, QC, H3G 1Y6, CA

Dr. Richard Wozniak
Professor
Department of Cell Biology
University of Alberta

“Sculpting the chromatin landscape: a role for nuclear pore complex assembly in chromatin structure”

In eukaryotic cells, the trafficking of macromolecules across the nuclear envelope, either into or out of the nucleus, is controlled by nuclear pore complexes (NPCs). NPCs are massive structures, ~65 MDa in mass and consisting of ~30 different proteins (termed nucleoporins) present in multiple copies. In addition to controlling transport, a growing body of literature has lead to the conclusion that NPCs also interact with chromatin and contribute to the regulation of gene expression. The mechanistic basis for these interactions, however, remains unclear. In recent studies, we have uncovered genetic and physical links between Nup170p, a nucleoporin critical for the assembly of NPCs, and proteins functioning in chromatin remodeling. On the basis these and other observations to be discussed, we hypothesize that Nup170p functions as a key component in the formation of the NPC and as a platform for the recruitment of chromatin remodeling complexes, in particular the RSC (Remodels Structure of Chromatin) complex, to sites of NPC formation. Here, we predict these proteins function in NPC assembly and in the formation, and/or maintenance, of chromatin domains in the vicinity of the NPC, including those functioning in the transcriptional repression of subtelomeric genes.

Makio, T., L. H. Stanton, C. C. Lin, D. S. Goldfarb, K. Weis, and R. W. Wozniak. 2009. J Cell Biol. 185:459-73.

Köhler, A. and E. Hurt. 2010. Mol Cell. 38:6-15.

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