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Scythe: a novel reaper‐binding apoptotic regulator
Author(s) -
Thress Kenneth,
Henzel William,
Shillinglaw Wendy,
Kornbluth Sally
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.21.6135
Subject(s) - biology , xenopus , microbiology and biotechnology , apoptosis , inhibitor of apoptosis domain , regulator , schneider 2 cells , caspase , dna fragmentation , drosophila melanogaster , programmed cell death , genetics , gene , rna , rna interference
Reaper is a central regulator of apoptosis in Drosophila melanogaster . With no obvious catalytic activity or homology to other known apoptotic regulators, reaper's mechanism of action has been obscure. We recently reported that recombinant Drosophila reaper protein induced rapid mitochondrial cytochrome c release, caspase activation and apoptotic nuclear fragmentation in extracts of Xenopus eggs. We now report the purification of a 150 kDa reaper‐interacting protein from Xenopus egg extracts, which we have named Scythe. Scythe is highly conserved among vertebrates and contains a ubiquitin‐like domain near its N‐terminus. Immunodepletion of Scythe from extracts completely prevented reaper‐induced apoptosis without affecting apoptosis triggered by activated caspases. Moreover, a truncated variant of Scythe lacking the N‐terminal domain induced apoptosis even in the absence of reaper. These data suggest that Scythe is a novel apoptotic regulator that is an essential component in the pathway of reaper‐induced apoptosis.