The histone H3-H4 tetramer is a copper reductase enzyme

Narsis Attar(University of California, Los Angeles), Oscar A. Campos(University of California, Los Angeles), Maria Vogelauer(University of California, Los Angeles), Chen Cheng(University of California, Los Angeles), Yong Xue(University of California, Los Angeles), Stefan Schmollinger(Abterra Biosciences (United States)), Łukasz Salwiński(University of California, Los Angeles), Nathan V. Mallipeddi(University of California, Los Angeles), Brandon A. Boone(University of California, Los Angeles), Linda Yen(University of California, Los Angeles), Sichen Yang(University of California, Los Angeles), Shannon Zikovich(University of California, Los Angeles), Jade Dardine(University of California, Los Angeles), Michael Carey(University of California, Los Angeles), Sabeeha Merchant(Abterra Biosciences (United States)), Siavash K. Kurdistani(University of California, Los Angeles)
Science
July 2, 2020
10.1126/science.aba8740
Cited by 117Open Access
Full Text

Abstract

Enzymatic activity of histones Eukaryotic histones serve as structural elements to package DNA. However, they contain a copper-binding site for which the biological relevance is unknown. Copper homeostasis is critical for several fundamental eukaryotic processes, including mitochondrial respiration. Attar et al. hypothesized that histones may play a critical role in cellular copper utilization (see the Perspective by Rudolph and Luger). Using a multifaceted approach ranging from in vitro biochemistry to in vivo genetic and molecular analyses, they found that the histone H3-H4 tetramer is an oxidoreductase enzyme that catalyzes reduction of cupric ions, thereby providing biologically usable cuprous ions for various cellular processes. This work opens a new front for chromatin biology, with implications for eukaryotic evolution and human biology and disease. Science , this issue p. 59 ; see also p. 33

Related Papers

No related papers found

Powered by citation graph analysis