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J Biol Chem, Vol. 275, Issue 1, 657-668, January 7, 2000
From the Department of Biochemistry, Medical College of Wisconsin,
Milwaukee, Wisconsin 53226
Several factors were evaluated to determine their
role in facilitating the presence of transcription-induced stresses in
a circular DNA. Transcription was done with T7 RNA polymerase in the
presence of E. coli topoisomerase I and closed circular
DNA. Positive stress was observed in hypotonic conditions or when one of the polyamines, spermidine or spermine, were present. Polycations such as polylysine, polyarginine, histone H1, histones H2A-H2B, and
protamine were observed to induce minimal positive stress. It is known
that polyamines influence DNA structure by causing both
self-association and sequence-specific structural alterations (polyamine-induced localized bending). Experimental evidence indicates that the likely cause of the positive stress is the induced bending. In
order to evaluate protein-mediated bending, transcription was done on
nucleosomes. A minimum of three nucleosomes on a DNA of 6055 bp was
sufficient to generate very high levels of positive stress. Histones
H3-H4 in the absence of H2A-H2B were responsible for this effect. Since
these histones by themselves are able to maintain negative coils on
DNA, it is concluded that protein-mediated bending is yet another
mechanism for placing rotational restriction on DNA. The bending of DNA
by either polyamines or histones is an effective mechanism for
promoting transcription-induced stresses at physiological ionic strength.
In Vitro Studies on the Maintenance of
Transcription-induced Stress by Histones and Polyamines*
*
This work was supported by National Science Foundation Grant
MCB-94056718.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 414-456-8776;
Fax: 414-456-6510.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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