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XB-ART-57157
Science 2020 Jul 03;3696499:59-64. doi: 10.1126/science.aba8740.
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The histone H3-H4 tetramer is a copper reductase enzyme.

Attar N , Campos OA , Vogelauer M , Cheng C , Xue Y , Schmollinger S , Salwinski L , Mallipeddi NV , Boone BA , Yen L , Yang S , Zikovich S , Dardine J , Carey MF , Merchant SS , Kurdistani SK .


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Eukaryotic histone H3-H4 tetramers contain a putative copper (Cu2+) binding site at the H3-H3' dimerization interface with unknown function. The coincident emergence of eukaryotes with global oxygenation, which challenged cellular copper utilization, raised the possibility that histones may function in cellular copper homeostasis. We report that the recombinant Xenopus laevis H3-H4 tetramer is an oxidoreductase enzyme that binds Cu2+ and catalyzes its reduction to Cu1+ in vitro. Loss- and gain-of-function mutations of the putative active site residues correspondingly altered copper binding and the enzymatic activity, as well as intracellular Cu1+ abundance and copper-dependent mitochondrial respiration and Sod1 function in the yeast Saccharomyces cerevisiae The histone H3-H4 tetramer, therefore, has a role other than chromatin compaction or epigenetic regulation and generates biousable Cu1+ ions in eukaryotes.

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Species referenced: Xenopus laevis
Genes referenced: sod1

References [+] :
Adamczyk, A zinc-finger like metal binding site in the nucleosome. 2007, Pubmed