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Papers In Press, published online ahead of print March 4, 2005
Department of Genetics, University of Wisconsin-Madison, Madison, WI 53706
Corresponding Author: vierstra{at}wisc.edu
Selective modification of proteins by ubiquitination is directed by diverse families of ubiquitin protein ligases (or E3s). A large collection of E3s use Cullins (CULs) as scaffolds to form multisubunit E3 complexes in which the CUL binds a target recognition subcomplex and the RBX1 docking protein which delivers the activated ubiquitin moiety. Arabidopsis and rice contain a large collection of CUL isoforms, indicating that multiple CUL-based E3s exist in plants. Here we show that Arabidopsis CUL3a and CUL3b associate with RBX1 and members of the Broad Complex/Tramtrack/Bric-a-Brac (BTB) protein family to form BTB E3s. Eighty BTB-domain containing genes were identified in the Arabidopsis genome, indicating that a diverse array of BTB E3s is possible. In addition to the BTB domain, the encoded proteins also contain various other interaction motifs that likely serve as target recognition elements. DNA microarray analyses show that BTB genes are expressed widely in the plant and that tissue-specific and isoform-specific patterns exist. Arabidopsis defective in both CUL3a and CUL3b are embryo lethal, indicating that the BTB-E3s are essential for plant development.
J. Biol. Chem, 10.1074/jbc.M413247200
Submitted on November 23, 2004
Revised on March 4, 2005
Accepted on March 4, 2005
Cullin 3A and B assemble with members of the broad complex/tramtrack/bric-A-brac (BTB)
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