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(Received for publication, June 20, 1997, and in revised form, July 16, 1997)
,
,
and
From the Copper is distributed to distinct localizations
in the cell through diverse pathways. We demonstrate here that the
delivery of copper to copper/zinc superoxide dismutase (SOD1) is
mediated through a soluble factor identified as Saccharomyces
cerevisiae LYS7 and human CCS (copper
chaperone for SOD). This factor is specific for
SOD1 and does not deliver copper to proteins in the mitochondria,
nucleus, or secretory pathway. Yeast cells containing a
lys7
Division of Toxicological Sciences,
Department of Environmental Health Sciences, Johns Hopkins University
School of Public Health, Baltimore, Maryland 21205 and the
¶ Edward Mallinckrodt Department of Pediatrics, Washington
University School of Medicine, St. Louis, Missouri 63110-1014
null mutation have normal levels of SOD1 protein,
but fail to incorporate copper into SOD1, which is therefore devoid of
superoxide scavenging activity. LYS7 and CCS specifically restore the
biosynthesis of holoSOD1 in vivo. Elucidation of the CCS
copper delivery pathway may permit development of novel therapeutic
approaches to human diseases that involve SOD1, including amyotrophic
lateral sclerosis.
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