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A more recent version of this article appeared on February 1, 2002
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Submitted on August 28, 2001
Revised on October 19, 2001
Accepted on November 1, 2001
1 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520 (present address: Fudan University, Department of Biochemistry, Shanghai 200433, China)
2 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520 (present address: Peking-Yale Joint Center for Plant Molecular Genetics and Agribiotechnology, Peking University, Beijing 100871, China)
3 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520
4 Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520 (present address: ZMBP - Center for Plant Molecular Biology, Universitaet Tuebingen, Tuebingen, Germany)
5 Department of Molecular, Cellular, and Developmental Biology, Yale University, Osborn Memorial Laboratories, Room 127, P.O. Box 208104, New Haven, CT 06520
* Corresponding author. E-mail address: ning.wei{at}yale.edu.
The COP9 signalosome (CSN) is a multi-functional protein complex essential for Arabidopsis development. One of its functions is to promote Rub1/Nedd8 de-conjugation from the cullin subunit of the SCF ubiquitin ligase. Little is known about the specific role of its 8 subunits in de-neddylation or any of the physiological functions of CSN. In the absence of CSN1 (the fus6 mutant), Arabidopsis CSN complex can not assemble, which destabilizes multiple CSN subunits and contributes, together with the loss of CSN1, to the phenotype of fus6. To distinguish CSN1 specific functions, we attempted to rescue the complex formation with deletion or point-mutation forms of CSN1 expressed as transgenes in fus6. We show that the central domain of CSN1 is critical for complex assembly while the C-terminal domain has a supporting role. By expressing the C231 fragment which contains the structural information but lacks the presumed functional domain located at the N-terminus, we have rescued the complex formation and restored the Rub1/Nedd8-deconjugation activity on cullins (fus6/C231). Nonetheless, fus6/C231 exhibits pleiotropic phenotype including photomorphogenic defects and growth arrest at seedling stage. We conclude that CSN1 N-terminal domain (CSN1N) is not required for the Rub1/Nedd8 de-conjugation activity of cullins, but contributes to a significant aspect of CSN functions that is essential for plant development.
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