Binding interaction of HMGB4 with cisplatin-modified DNA.

ABSTRACT: Proteins in the HMG family are important transcription factors. They recognize cisplatin-damaged DNA lesions with a structure-specific preference and account for more than 70% of all proteins that interact with the cisplatin 1,2-intrastrand d(GpG) cross-link. HMGB4, a new member of the mammalian HMGB protein family expressed preferentially in the testis, was generated recombinantly, and its interactions with cisplatin-modified DNA were investigated in vitro. The binding affinities of the two individual DNA-binding domains of HMGB4 to DNA carrying a cisplatin 1,2-intrastrand d(GpG) cross-link are weaker than those of the DNA-binding domains of HMGB1. Full-length HMGB4, however, has a 28-fold stronger binding affinity (K(d) = 4.35 nM) for the platinated adduct compared to that of HMGB1 (K(d)

SUBMITTER: Park S 

PROVIDER: S-EPMC3448822 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature