Nucleic Acids, Protein Synthesis, and Molecular Genetics
Modulation of Chromatin Folding by Histone Acetylation *

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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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This work was supported by British Columbia Health Care Research Foundation Grants 19 (93-1)-3 (94-1) (to J. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

© 1995 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.