A pathogenic role for histone H3 copper reductase activity in a yeast model of Friedreich’s ataxia

Campos, Oscar A.; Attar, Narsis; Cheng, Chen; Vogelauer, Maria; Mallipeddi, Nathan V.; Schmollinger, Stefan; Matulionis, Nedas; Christofk, Heather R.; Merchant, Sabeeha S.; Kurdistani, Siavash K.

doi:10.1126/sciadv.abj9889

Title: A pathogenic role for histone H3 copper reductase activity in a yeast model of Friedreich’s ataxia

Journal Article · 16 December 2021 · Science Advances

DOI: https://doi.org/10.1126/sciadv.abj9889 · OSTI ID:1889830

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Univ. of California, Los Angeles, CA (United States)
Univ. of California, Berkeley, CA (United States)
Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Environmental Genomics and Systems Biology

Disruptions to iron-sulfur (Fe-S) clusters, essential cofactors for a broad range of proteins, cause widespread cellular defects resulting in human disease. A source of damage to Fe-S clusters is cuprous (Cu¹⁺) ions. Since histone H3 enzymatically produces Cu¹⁺ for copper-dependent functions, we asked whether this activity could become detrimental to Fe-S clusters. Here, we report that histone H3–mediated Cu¹⁺ toxicity is a major determinant of cellular functional pool of Fe-S clusters. Inadequate Fe-S cluster supply, due to diminished assembly as occurs in Friedreich’s ataxia or defective distribution, causes severe metabolic and growth defects in Saccharomyces cerevisiae. Decreasing Cu¹⁺ abundance, through attenuation of histone cupric reductase activity or depletion of total cellular copper, restored Fe-S cluster–dependent metabolism and growth. Our findings reveal an interplay between chromatin and mitochondria in Fe-S cluster homeostasis and a potential pathogenic role for histone enzyme activity and Cu¹⁺ in diseases with Fe-S cluster dysfunction.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: National Cancer Institute (NCI); National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1889830

Journal Information:: Science Advances, Journal Name: Science Advances Journal Issue: 51 Vol. 7; ISSN 2375-2548

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: English

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