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Nickel binding sites in histone proteins

Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Solinas, Costantino and Medici, Serenella (2012) Nickel binding sites in histone proteins. In: AsBIC VI: the 6. Asian biological inorganic chemistry conference, November 5-8, 2012, Hong-Kong, China. [S.l.] Conference or Workshop Item.

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Nickel compounds are well known as human carcinogens, though the molecular events that are responsible for this are not well understood.
It has been proposed that a crucial element in the mechanism of carcinogenesis is the binding of Ni(II) ions within the cell nucleus. It is known that DNA polymer binds Ni(II) only weakly, leaving the proteins of the cell nucleus as the likely Ni(II) targets. Being histone proteins the most abundant among them, they can be considered the primary sites for nickel binding. Here we describe the interactions of nickel with histone H4, core tetramer (H3-H4)2 and several peptide fragments which have been selected as the candidates for specific binding sites in the histone octamer. The results allowed us to propose several mechanisms of nickel induced damage resulting from metal coordination, including structural changes of histone proteins, as well as nucleobase oxidation and sequence-specific histone hydrolysis.
The aim of the present work is to provide a comprehensive overview of literature dealing with nickel coordination to histone proteins and its link with nickel involvement in toxicity and carcinogenicity.

Item Type:Conference or Workshop Item (Poster)
ID Code:8964
Uncontrolled Keywords:Histone, cancer, nickel
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
Deposited On:10 May 2013 08:49

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