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Volume 270, Number 30, Issue of July 28, pp. 17923-17928, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Modulation of Chromatin Folding by Histone Acetylation

(Received for publication, May 22, 1995; and in revised form, June 1, 1995)

Marta Garcia-Ramirez Corinne Rocchini Juan Ausio

From the  (1)Institut de Recerca Oncologica, Hospital Duran Reynals, Generalital de Catalunya, Carretera de Castelldefels s/n Barcelona, E-08907 Spain and the (2)Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada

A homogeneous oligonucleosome complex was prepared by reconstitution of highly hyperacetylated histone octamers onto a linear DNA template consisting of 12 tandemly arranged 208-base pair fragments of the 5 S rRNA gene from the sea urchin Lytechinus variegatus. The ionic strength-dependent folding of this oligonucleosome assembly was monitored by sedimentation velocity and electron microscopy. Both types of analysis indicate that under ionic conditions resembling those found in the physiological range and in the absence of histone H1, the acetylated oligonucleosome complexes remain in an extended conformation in contrast to their nonacetylated counterparts. The implications of this finding in the context of a multistate model of chromatin folding (Hansen, J. C., and Ausio, J.(1992) TIBS 197, 187-191) as well as its biological relevance are discussed.




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