Faculty Opinions recommendation of 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.Copyright © 2020, American Association for the Advancement of Science. PMID: 32631887 Funding information This work was supported by: NCI NIH HHS, United States Grant ID: F30 CA186619 NCI NIH HHS, United States Grant ID: R01 CA178415 NIAID NIH HHS, United States Grant ID: P30 AI028697 NCI NIH HHS, United States Grant ID: P30 CA016042 NIGMS NIH HHS, United States Grant ID: T32 GM008042 NCI NIH HHS, United States Grant ID: R03 CA188592 NIGMS NIH HHS, United States Grant ID: R01 GM042143 NIGMS NIH HHS, United States Grant ID: T32 GM007185 NIGMS NIH HHS, United States Grant ID: R01 GM123126 NIGMS NIH HHS, United States Grant ID: R01 GM074701 NIGMS NIH HHS, United States Grant ID: R37 GM042143 More Less keyboard_arrow_down