Interaction of Nickel(II) with histones: in vitro binding of nickel(II) to the core histone tetramer.
The absorption spectra of Ni(II) bound to the core histone tetramer, (H3-H4)2, of chicken erythrocytes in 500 mM NaCl + 100 mM phosphate (pH 7.4) were recorded. A charge transfer band was seen at 317 nm, characteristic of a bond between Ni(II) and the sulfur atom of Cys-110 of histone H3. The conditional affinity constants for Ni(II) binding at pH 7.4 for low and high Ni(II) saturation (log Kc = 4.26 +/- 0.02 and 5.26 +/- 0.11 M-1, respectively) were calculated from spectrophotometric titrations with the use of this band. The binding of Ni(II) to (H3-H4)2 is proposed to involve the Cys-110 and His-113 of different H3 molecules within the tetramer. The competition between histones and low-molecular-weight chelators for Ni(II) in the cell nucleus, histidine and glutathione, is discussed on the basis of the above results, indicating that histone H3 is very likely to bind Ni(II) dissolved intracellularly from phagocytosed particulate nickel compounds.
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Laboratory of Comparative Carcinogenesis, National Cancer Institute, FCRDC, Frederick, Maryland, 21702, USA.
Karantza
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Moudrianakis
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Kasprzak
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D000818:Animals; D001667:Binding, Competitive; D002645:Chickens; D006657:Histones / Q000378:metabolism*; D009532:Nickel / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
D006657:Histones; D011108:Polymers; D009532:Nickel