Your browser doesn't support javascript.
loading
The histone H3-H4 tetramer is a copper reductase enzyme.
Attar, Narsis; Campos, Oscar A; Vogelauer, Maria; Cheng, Chen; Xue, Yong; Schmollinger, Stefan; Salwinski, Lukasz; Mallipeddi, Nathan V; Boone, Brandon A; Yen, Linda; Yang, Sichen; Zikovich, Shannon; Dardine, Jade; Carey, Michael F; Merchant, Sabeeha S; Kurdistani, Siavash K.
Afiliação
  • Attar N; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Campos OA; Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Vogelauer M; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Cheng C; Molecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Xue Y; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Schmollinger S; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Salwinski L; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Mallipeddi NV; Institute for Genomics and Proteomics, Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Boone BA; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Yen L; UCLA-DOE Institute for Genomics and Proteomics, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Yang S; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Zikovich S; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Dardine J; Department of Molecular, Cell, and Developmental Biology, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Carey MF; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Merchant SS; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
  • Kurdistani SK; Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095, USA.
Science ; 369(6499): 59-64, 2020 07 03.
Article em En | MEDLINE | ID: mdl-32631887
ABSTRACT
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.
Assuntos
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Histonas / Cobre / Multimerização Proteica Idioma: En Ano de publicação: 2020 Tipo de documento: Article
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Histonas / Cobre / Multimerização Proteica Idioma: En Ano de publicação: 2020 Tipo de documento: Article