Zoroddu, Maria Antonietta and Peana, Massimiliano Francesco and Medici, Serenella (2010) Ni(II)-Histone H4 interactions: structural modifications. In: 21. Spanish-Italian Congress on Thermodynamics of Metal Complexes ISMEC 2010, 7-11 June 2010, Bilbao, Spain. [S.l.], Universidad del Paìs Vasco. p. 52. Conference or Workshop Item.
It is known that nickel participates to carcinogenic processes through mechanisms interfering with several cellular targets; among them, histone H4 has been recently identified. Histones are nuclear proteins that package and organize DNA into nucleosomes and chromatin, but they are also involved in gene regulation and transcription. By undergoing post-translational modifications, such as acetylation, methylation and phosphorylation, they change chromatin structure helping gene transcription or inhibition. Nickel showed to be in vivo a potent inhibitor of histone H4 acetylation. Acetylation causes important structural modifications in histones: for instance, it increases the α-helix content, thus decreasing the length of the histone tail and affecting the transcription mechanisms.
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