The histone H3-H4 tetramer is a copper reductase enzyme.

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.
Mesh Terms:
Animals, Biocatalysis, Catalytic Domain, Copper, Gain of Function Mutation, Histones, Mitochondria, Nuclear Proteins, Oxidoreductases, Protein Multimerization, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Superoxide Dismutase-1, Transcription Factors, Xenopus laevis
Date: Dec. 03, 2019
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