The histone H3-H4 tetramer is a copper reductase enzyme-Reference-Cited by-同舟云学术

The histone H3-H4 tetramer is a copper reductase enzyme

Published:2020-07-03 Issue:6499 Volume:369 Page:59-64
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Attar Narsis¹²^ORCID,Campos Oscar A.¹²^ORCID,Vogelauer Maria¹^ORCID,Cheng Chen¹,Xue Yong¹,Schmollinger Stefan³^ORCID,Salwinski Lukasz¹⁴^ORCID,Mallipeddi Nathan V.¹^ORCID,Boone Brandon A.¹^ORCID,Yen Linda⁵^ORCID,Yang Sichen¹^ORCID,Zikovich Shannon¹,Dardine Jade¹^ORCID,Carey Michael F.¹²^ORCID,Merchant Sabeeha S.³^ORCID,Kurdistani Siavash K.¹²⁶^ORCID

Affiliation:

1. Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.

2. Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.

3. Institute for Genomics and Proteomics, Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA.

4. UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.

5. Department of Molecular, Cell, and Developmental Biology, University of California Los Angeles, Los Angeles, CA 90095, USA.

6. Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.

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

Funder

National Institutes of Health

U.S. Department of Energy

W.M. Keck Foundation

University of California, Los Angeles

National Cancer Institute

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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1. Structure of histone-based chromatin in Archaea