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Repair of Cisplatin−DNA Adducts by the Mammalian Excision Nuclease

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 1996, 35, 31, 10004-10013
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    Repair of Cisplatin−DNA Adducts by the Mammalian Excision Nuclease†
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    Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, and Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599-7260
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    Biochemistry

    Cite this: Biochemistry 1996, 35, 31, 10004–10013
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    https://doi.org/10.1021/bi960453+
    Published August 6, 1996
    Copyright © 1996 American Chemical Society
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    Abstract

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    Nucleotide excision repair is one of the many cellular defense mechanisms against the toxic effects of cisplatin. An in vitro excision repair assay employing mammalian cell-free extracts was used to determine that the 1,2-d(ApG) intrastrand cross-link, a prevalent cisplatin−DNA adduct, is excised by the excinuclease from a site-specifically modified oligonucleotide 156 base pairs in length. Repair of the minor interstrand d(G)/d(G) cross-link was not detected by using this system. Proteins containing the high mobility group (HMG) domain DNA-binding motif, in particular, rat HMG1 and a murine testis-specific HMG-domain protein, specifically inhibit excision repair of the intrastrand 1,2-d(GpG) and -d(ApG) cross-links. This effect was also exhibited by a single HMG domain from HMG1. Similar inhibition of repair of a site-specific 1,2-d(GpG) intrastrand cross-link by an HMG-domain protein also occurred in a reconstituted system containing highly purified repair factors. These results indicate that HMG-domain proteins can block excision repair of the major cisplatin−DNA adducts and suggest that such an activity could contribute to the unique sensitivity of certain tumors to the drug. The reconstituted excinuclease was more efficient at excising the 1,3-d(GpTpG) intrastrand adduct than either the 1,2-d(GpG) or d(ApG) intrastrand adducts, in agreement with previous experiments using whole cell extracts [Huang, J.-C., Zamble, D. B., Reardon, J. T., Lippard, S. J., Sancar, A. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10394−10398]. This result suggests that structural differences among the platinated DNA substrates, and not the presence of unidentified cellular factors, determine the relative excision repair rates of cisplatin−DNA intrastrand cross-links in the whole cell extracts.

    Copyright © 1996 American Chemical Society

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    †

     This work was supported by Grant CA34992 to S.J.L. from the National Cancer Institute and by Grant GM32833 to A.S. from the National Institute of General Medical Sciences. D.B.Z. is a Howard Hughes Medical Insitute predoctoral fellow. D. M. is supported by Grant DR-1319 from the Cancer Research Division of the Damon Runyon−Walter Winchell Foundation.

    ‡

     Massachusetts Institute of Technology.

    §

     University of North Carolina.

    *

     To whom correspondence should be addressed.

    ✗

     Abstract published in Advance ACS Abstracts, July 1, 1996.

    Cited By

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    This article is cited by 239 publications.

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    Biochemistry

    Cite this: Biochemistry 1996, 35, 31, 10004–10013
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    https://doi.org/10.1021/bi960453+
    Published August 6, 1996
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