High affinity MAR-DNA binding is a common property of murine and human mutant p53
✍ Scribed by Katrin Will; Gabriele Warnecke; Nils Albrechtsen; Teni Boulikas; Wolfgang Deppert
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 179 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0730-2312
No coin nor oath required. For personal study only.
✦ Synopsis
We recently reported that murine MethA mutant but not wild-type p53 specifically binds to MAR-DNA elements (MARs) with high affinity. Here we show that this DNA binding activity is exerted not only by MethA mutant p53 but also by other murine mutant p53 proteins isolated from the transformed murine BALB/c cell lines 3T3tx and T3T3 and differing in their conformational status. High affinity MAR-DNA binding was not restricted to the XbaI-IgE-MAR-DNA fragment from the murine immunoglobulin heavy chain gene enhancer locus : J Biol Chem 262:5394-5397] used in previous studies, as MethA p53 also specifically interacted with other A/T-rich bona fide MARs. Not only murine but also human mutant p53 proteins carrying the mutational hot spot amino acid exchanges 175Arg=His, 273Arg=Pro, or 273Arg=His bound to the XbaI-IgE-MAR-DNA fragment. We therefore conclude that high affinity MAR-DNA binding is a property common to a variety of mutant p53 proteins.