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J. Biol. Chem., Vol. 276, Issue 42, 38774-38780, October 19, 2001
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,
From the Department of Chemistry, Massachusetts Institute of
Technology, Cambridge, Massachusetts 02139
The results presented describe the effects
of various spectator ligands, attached to a platinum 1,2-intrastand
d(GpG) cross-link in duplex DNA, on the binding of high mobility group
box (HMGB) domains and the TATA-binding protein (TBP). In addition to
cisplatin-modified DNA, 15-base pair DNA probes modified by
{Pt(1R,2R-diaminocyclohexane)}2+,
cis-{Pt(NH3)(cyclohexylamine)}2+,
{Pt(ethylenediamine)}2+,
cis-{Pt(NH3)(cyclobutylamine)}2+,
and cis-{Pt(NH3)(2-picoline)}2+
were examined. Electrophoretic mobility shift assays show that both the A and B domains of HMGB1 as well as TBP discriminate between
different platinum-DNA adducts. HMGB1 domain A is the most sensitive to
the nature of the spectator ligands on platinum. The effect of the
spectator ligands on protein binding also depends highly on the base
pairs flanking the platinated d(GpG) site. Double-stranded
oligonucleotides containing the AG*G*C sequence, where the asterisks
denote the sites of platination, with different spectator ligands are
only moderately discriminated by the HMGB proteins and TBP, but the
recognition of dsTG*G*A is highly dependent on the ligands. The effects
of HMGB1 overexpression in a BG-1 ovarian cancer cell line, induced by
steroid hormones, on the sensitivity of cells treated with
[Pt(1R,2R-diaminocyclohexane)Cl2] and
cis-[Pt(NH3)(cyclohexylamine)Cl2]
were also examined. The results suggest that HMGB1 protein levels
influence the cellular processing of
cis-{Pt(NH3)- (cyclohexylamine)}2+,
but not
{Pt((1R,2R)-diaminocyclohexane)}2+,
DNA lesions. This result is consistent with the observed binding of
HMGB1a to platinum-modified dsTG*G*A probes but not with the binding
affinity of HMGB1a and HMGB1 to platinum-damaged dsAG*G*C oligonucleotides. These experiments reinforce the importance of sequence context in platinum-DNA lesion recognition by cellular proteins.
The on-line version of this article (available at
http://www.jbc.org) contains Tables S1 and S2 and Fig. S1.
Anna Fuller Fund Postdoctoral Fellow.
§
National Institutes of Health Postdoctoral Fellow.
¶
To whom correspondence should be addressed. Tel.:
617-253-1892; Fax: 617-258-8150; E-mail:
lippard@lippard.mit.edu.
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