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Journal of Cell Science, Vol 96, 439-450, Copyright © 1990 by Company of Biologists
Submitted on December 7, 1989
Accepted on March 26, 1990
1 Swiss Institute for Experimental Cancer Research (ISREC), Chemin des Boveresses 155, CH-1066 Epalinges/Lausanne, Switzerland
Author for correspondence
The yeast nuclear scaffold has been shown to bind with high affinity to genomic sequences that permit autonomous DNA replication of plasmids (ARS elements). We describe here conditions for the isolation of a histone-free nuclear substructure, the nuclear scaffold, from Saccharomyces cerevisiae. We examine the protein composition of this structure, and the conditions under which topoisomerase II, the nuclear factor RAP-1 and RNA polymerase II cofractionate with the scaffold. We find that exposure of nuclei to a combined metal and heat treatment (0.5mH Cu2+, 37°C) prior to detergent extraction is required for effective stabilization of these proteins with the scaffold. Electron microscopy of the residual nuclei extracted with non-ionic detergents shows the absence of a typical peripheral lamina structure.
Key words: nuclear scaffold, nuclear matrix, topoisomerase II, RAP-1, S. cerevisia
Submitted on December 7, 1989
Accepted on March 26, 1990
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