Nickel has been shown to be an essential trace element involved in the metabolism of several species of bacteria, archea, plant and may yet be found to play a role in the metabolism of higher organisms1 . However, the carcinogenicity of certain nickel compounds has been confirmed by the combination of epidemiological evidence in humans and carcinogenesis bioassays in animals 2. The molecular mechanisms of nickel-induced carcinogenesis include interactions of this metal with major chromatin components causing alterations in gene expression rather than by direct DNA damage. We have previously reported that nickel is a potent suppressor of histone H4 acetylation, in both yeast and mammalian cells 3-5. It has preference to specific lysine residues in the N-terminal tail of histone H4, in which the sites of acetylation are clustered. Here we present our recent results on the coordination ability of Ni(II) to the N-terminal tail of Histone H4 using NMR spectroscopy. A series of 1D, 2D Tocsy and Noesy 1H NMR spectra of the tail with increasing nickel concentration to the final molar ratio 1:1, were acquired

NMR study of Nickel binding to N-tail of Histone H4 / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella. - (2005), pp. 1-1. ((Intervento presentato al convegno First European Conference on Chemistry for Life Science, Understanding the Chemical Mechanisms of Life tenutosi a Rimini, Italia nel 4-8 Ottobre 2005.

NMR study of Nickel binding to N-tail of Histone H4

ZORODDU, Maria Antonietta;PEANA, Massimiliano Francesco;MEDICI, Serenella
2005-01-01

Abstract

Nickel has been shown to be an essential trace element involved in the metabolism of several species of bacteria, archea, plant and may yet be found to play a role in the metabolism of higher organisms1 . However, the carcinogenicity of certain nickel compounds has been confirmed by the combination of epidemiological evidence in humans and carcinogenesis bioassays in animals 2. The molecular mechanisms of nickel-induced carcinogenesis include interactions of this metal with major chromatin components causing alterations in gene expression rather than by direct DNA damage. We have previously reported that nickel is a potent suppressor of histone H4 acetylation, in both yeast and mammalian cells 3-5. It has preference to specific lysine residues in the N-terminal tail of histone H4, in which the sites of acetylation are clustered. Here we present our recent results on the coordination ability of Ni(II) to the N-terminal tail of Histone H4 using NMR spectroscopy. A series of 1D, 2D Tocsy and Noesy 1H NMR spectra of the tail with increasing nickel concentration to the final molar ratio 1:1, were acquired
NMR study of Nickel binding to N-tail of Histone H4 / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella. - (2005), pp. 1-1. ((Intervento presentato al convegno First European Conference on Chemistry for Life Science, Understanding the Chemical Mechanisms of Life tenutosi a Rimini, Italia nel 4-8 Ottobre 2005.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11388/71678
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact