Although nickel has been shown to be an essential trace element involved in the metabolism of bacteria, archaea, plants and higher organisms, the carcinogenicity of certain nickel compounds has been confirmed by the combination of epidemiological evidence in humans and carcinogenesis bioassays in animals and it is probably due to alteration in gene expression rather than by direct DNA damage.
We have previously reported that Ni(II) is a potent suppressor of histone H4 acetyaltion, in both yeast and mammalian cells.
Here we present our recent results on the coordination ability of Ni(II) to the N-terminal tail of HIstone H4 achieved by the use of NMR techiniques like 1d, 2D Tocsy and Noesy H NMR experiments. A structural model of the peptide-Ni(II) complex has been calculated, pointing out the important structural changes occurring to the peptide upon coordination
