NDLI: Nickel binding to histone H4

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Peana, Massimiliano Medici, Serenella Costa, Max Casella, Luigi Monzani, Enrico Zoroddu, Maria Antonietta
Description	Author Affiliation: Zoroddu MA ( Department of Chemistry & Pharmacy Faculty, University of Sassari, via Vienna 2, 07100, Sassari, Italy. zoroddu@uniss.it)
Abstract	Nickel compounds influence carcinogenesis by interfering with a variety of cellular targets. It has been found that nickel is a potent inhibitor in vivo of histone H4 acetylation , in both yeast and mammalian cells. It has preference to specific lysine residues in the H4 N-terminal $-S_{1}GRGK_{5}GGK_{8}GLGK_{12}GGAK_{16}RH_{18}RKVL_{22}$ tail, in which the sites of acetylation are clustered. About the nature of the structural changes induced by histone acetylation on H4, it has been recently demonstrated that acetylation induces an increase in α-helical conformation of the acetylated N-terminal tail of H4. It causes a shortening of the tail and, such an effect, may have an important structural and functional implication as a mechanism of transcriptional regulation. Here we report a study on the conformational changes induced by carcinogenic nickel compounds on the histone H4 protein . From a circular dichroism study we found that nickel is able to induce a secondary structure in the protein . In particular, nickel has the same effect as acetylation : it induces an increase in α-helical conformation of the non-acetylated histone H4. The α-helical increase that occurs upon nickel interaction with histone H4 should decrease the ability of histone acetyl transferase to recognize and bind to the histone tail and thus affect the ability of the enzyme to further modify the lysine residues. The shortening of the distance between adjacent amino acids , caused by the translation from an extended to a helical conformation, could disrupt the histone recognition motif; this may eventually compromise the entire “ histone code”.
ISSN	14779226
Issue Number	3
Volume Number	39
e-ISSN	13645447
Journal	Dalton Trans.
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2010-01-21
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Carcinogens Metabolism Histones Nickel Amino Acid Sequence Toxicity Circular Dichroism Chemistry Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Secondary Drug Effects Journal Article
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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