Characterization of DNA-protein cross-links formed by treatment of L1210 cells and nuclei with bis(2-chloroethyl)methylamine (nitrogen mustard).
Proteins cross-linked to DNA after nitrogen mustard (HN2) treatment of cells or isolated nuclei were purified in CsCl gradients. The protein-DNA cross-links could be cleaved by incubation in dilute acid and could be stabilized by alkali pretreatment. These results indicate that proteins cross-linked to DNA by HN2 are bound to alkylated purines. Analysis of the DNA-bound proteins on NaDodSO4-polyacrylamide gels showed that primarily large nonhistone proteins are cross-linked to DNA in cells treated with HN2. Very little if any histone is cross-linked to the DNA. Comparison of DNA bound proteins from HN2-treated cells and HN2-treated nuclei showed that in general the same proteins are linked to DNA in both cases, but some qualitative and quantitative differences exist.
D000478:Alkylation; D000818:Animals; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism*; D004273:DNA, Neoplasm / Q000378:metabolism*; D007700:Kinetics; D007939:Leukemia L1210 / Q000378:metabolism*; D008466:Mechlorethamine / Q000494:pharmacology*; D009363:Neoplasm Proteins / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism; D011485:Protein Binding
D004273:DNA, Neoplasm; D009363:Neoplasm Proteins; D009698:Nucleoproteins; D008466:Mechlorethamine