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Vol. 13, Issue 2, 493-502, February 2002
and
*Genome Damage and Stability Centre, School of Biological
Sciences, University of Sussex, Falmer, Sussex, BN1 9RR, United
Kingdom; and Department of Medical Microbiology, School of Basic
Medical Sciences, West China University of Medical Sciences, Chengdu
610041, People's Republic of China
The COP9/signalosome complex is highly conserved in evolution and
possesses significant structural similarity to the 19S regulatory lid
complex of the proteasome. It also shares limited similarity to the
translation initiation factor eIF3. The signalosome interacts with
multiple cullins in mammalian cells. In the fission yeast Schizosaccharomyces pombe, the Csn1 subunit is required
for the removal of covalently attached Nedd8 from Pcu1, one of three
S. pombe cullins. It remains unclear whether this
activity is required for all the functions ascribed to the signalosome.
We previously identified Csn1 and Csn2 as signalosome subunits in
S. pombe. csn1 and csn2 null mutants are
DNA damage sensitive and exhibit slow DNA replication. Two further
putative subunits, Csn4 and Csn5, were identified from the S.
pombe genome database. Herein, we characterize null mutations
of csn4 and csn5 and demonstrate that
both genes are required for removal of Nedd8 from the S. pombe cullin Pcu1 and that their protein products associate
with Csn1 and Csn2. However, neither csn4 nor
csn5 null mutants share the csn1 and
csn2 mutant phenotypes. Our data suggest that the subunits of the signalosome cannot be considered as a distinct functional unit and imply that different subunits of the signalosome mediate distinct functions.
Present address: ESBA Tech AG,
Winterhurerstr. 190, CH-8057 Zurich, Switzerland.
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