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Vol. 16, No. 5, pp. 554-559, March 1, 2002
1 Department of Molecular, Cellular, and Developmental
Biology, Yale University, New Haven, Connecticut 06520, USA;
2 Genomic Sciences Center, RIKEN2-1 Hirosawa,
Wako-shi, Saitama 351-0198, Japan
A group of evolutionarily conserved pleiotropic COP/DET/FUS
proteins was initially defined by their ability to repress
photomorphogenesis in Arabidopsis. It was proposed that
this regulation be mediated by targeting degradation of key cellular
regulators that promote photomorphogenesis. Among them, COP1 and the
COP9 signalosome have been hypothesized to fulfill the roles as an
ubiquitin ligase (E3) and an essential E3 modulator. Here we report
that COP10 encodes a protein similar to ubiquitin-conjugating
enzyme (E2) variant proteins (UEV). COP10 is part of a nuclear protein
complex and capable of directly interacting with both COP1 and the COP9 signalosome. Our data indicates that COP10 defines a possible E2
activity, thus validating the working hypothesis that the pleiotropic COP/DET/FUS group of proteins defined a protein ubiquitination pathway.
[Key Words: EUV; ubiquitination; proteasome; Arabidopsis; photomorphogenesis; protein degradation]
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