The Octapeptidic End of the C-Terminal Tail of Histone H2A Is Cleaved Off in Cells Exposed to Carcinogenic Nickel(II)

We have demonstrated previously that Ni(II) binds to the C-terminal −TESHHKAKGK motif of isolated bovine histone H2A. At physiological pH, the bound Ni(II) assists in hydrolysis of the E−S peptide bond in this motif that results in a cleavage of the terminal octapeptide SHHKAKGK off the histone'...

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