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A more recent version of this article appeared on February 1, 2002
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Submitted on July 11, 2001
Revised on October 23, 2001
Accepted on November 1, 2001
1 Genome Damage and Stability Centre, School of Biological Sciences, Sussex University, Falmer, Sussex, BN1 9RR. U.K. (present address: ESBA Tech AG Winterhurerstr. 190, CH-8057 Zurich, Switzerland)
2 Genome Damage and Stability Centre, School of Biological Sciences, Sussex University, Falmer, Sussex, BN1 9RR. U.K. (present affiliation also includes: Department of Medical Microbiology, School of Basic Medical Sciences, West China University of Medical Sciences, Chengdu 610041, PR China)
3 Genome Damage and Stability Centre, School of Biological Sciences, Sussex University, Falmer, Sussex, BN1 9RR. U.K.
* Corresponding author. E-mail address: a.m.carr{at}sussex.ac.uk.
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 S. pombe, the Csn1 subunit is required for the removal of covalently attached Nedd8 from Pcu1, one of three S. pombe cullins. It remains unclear if 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. Here we characterise 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.
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