High mobility group proteins 1 and 2 recognize chromium-damaged DNA |
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Authors: | Wang JF; Bashir M; Engelsberg BN; Witmer C; Rozmiarek H; Billings PC |
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Institution: | Department of Pathology, School of Dental Medicine, University of Pennsylvania, Philadelphia 19104-6002, USA. |
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Abstract: | Chromium (Cr) is a human carcinogen and a potent DNA damaging agent.
Incubation of DNA with CrCl3 resulted in dose-dependent binding of Cr to
DNA and, at concentrations >20 microM, altered the electrophoretic
mobility of a 100 bp oligonucleotide. We also demonstrate that high
mobility group (HMG) proteins 1 and 2 bind Cr-damaged DNA (Cr-DNA). Protein
binding was lesion density-dependent, with maximal binding to DNA treated
with 100 microM CrCl3. HMG2 binds to Cr-DNA with a calculated Kd of
approximately 10(-9) M. These proteins also bound DNA obtained from
chromate-treated cells. These results suggest that the covalent attachment
of Cr to DNA induces alterations in DNA structure which are recognized by
HMG1 and HMG2. Therefore, these proteins may function as Cr-damaged DNA
recognition proteins in vivo and as a consequence of binding, may play a
role in directing the cellular response to Cr-DNA adduct formation.
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