CCS1 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.
Bowman S, Churcher C, Badcock K, Brown D, Chillingworth T, Connor R, Dedman K, Devlin K, Gentles S, Hamlin N, Hunt S, Jagels K, Lye G, Moule S, Odell C, Pearson D, Rajandream M, Rice P, Skelton J, Walsh S, Whitehead S, Barrell B
Nature387(6632 Suppl)90-3(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Data suggest that Ccs1 activates immature Sod1 by delivering copper and facilitating oxidation of intramolecular disulfide bond in Sod1; Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on the apoenzyme. (Ccs1 = copper chaperone for superoxide dismutase; Sod1 = copper-zinc superoxide dismutase)
Title: Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.

Data show that the aging process increased the DNA damage rates 3-fold in the wild type and more than 5-fold in superoxide dismutases sod1Delta, sod2Delta, and molecular chaperone ccs1Delta mutant cells.
Title: Absence of superoxide dismutase activity causes nuclear DNA fragmentation during the aging process.

CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition.
Title: Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes.

Localization of the reduced, Ccs1-independent forms of Sod1 relied on Mia40, an essential component of the mitochondrial intermembrane space import and assembly pathway
Title: Mia40 and MINOS act in parallel with Ccs1 in the biogenesis of mitochondrial Sod1.

The Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in the copper chaperone Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.
Title: Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system.