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Mol Cell Biol, August 1998, p. 4629-4638, Vol. 18, No. 8
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Disruption of Higher-Order Folding by Core Histone
Acetylation Dramatically Enhances Transcription of Nucleosomal Arrays
by RNA Polymerase III
Christin
Tse,1
Takashi
Sera,2
Alan P.
Wolffe,2 and
Jeffrey
C.
Hansen1 *
Department of Biochemistry, The University of
Texas Health Science Center at San Antonio, San Antonio, Texas
78284-7760,1 and
Laboratory of Molecular
Embryology, National Institute of Child Health and Human
Development, National Institutes of Health, Bethesda, Maryland
20892-54312
Received 3 April 1998/Returned for modification 18 May
1998/Accepted 20 May 1998
We have examined the effects of core histone acetylation on the
transcriptional activity and higher-order folding of defined 12-mer
nucleosomal arrays. Purified HeLa core histone octamers containing an
average of 2, 6, or 12 acetates per octamer (8, 23, or 46% maximal
site occupancy, respectively) were assembled onto a DNA template
consisting of 12 tandem repeats of a 208-bp Lytechinus 5S
rRNA gene fragment. Reconstituted nucleosomal arrays were transcribed
in a Xenopus oocyte nuclear extract and analyzed by
analytical hydrodynamic and electrophoretic approaches to determine the
extent of array compaction. Results indicated that in buffer containing
5 mM free Mg2+ and 50 mM KCl, high levels of acetylation
(12 acetates/octamer) completely inhibited higher-order folding and
concurrently led to a 15-fold enhancement of transcription by RNA
polymerase III. The molecular mechanisms underlying the acetylation
effects on chromatin condensation were investigated by analyzing the
ability of differentially acetylated nucleosomal arrays to fold and
oligomerize. In MgCl2-containing buffer the folding of
12-mer nucleosomal arrays containing an average of two or six acetates
per histone octamer was indistinguishable, while a level of 12 acetates
per octamer completely disrupted the ability of nucleosomal arrays to
form higher-order folded structures at all ionic conditions tested. In
contrast, there was a linear relationship between the extent of histone
octamer acetylation and the extent of disruption of Mg2+-dependent oligomerization. These results have yielded
new insight into the molecular basis of acetylation effects on both
transcription and higher-order compaction of nucleosomal arrays.
*
Corresponding author. Mailing address: Department of
Biochemistry, The University of Texas Health Science Center at San
Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78284-7760. Phone: (210) 567-6980. Fax: (210) 567-6595. E-mail:
hansen{at}bioc02.uthscsa.edu.
Mol Cell Biol, August 1998, p. 4629-4638, Vol. 18, No. 8
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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