RRC ID 598
Author Gingerich DJ, Gagne JM, Salter DW, Hellmann H, Estelle M, Ma L, Vierstra RD.
Title Cullins 3a and 3b assemble with members of the broad complex/tramtrack/bric-a-brac (BTB) protein family to form essential ubiquitin-protein ligases (E3s) in Arabidopsis.
Journal J. Biol. Chem.
Abstract 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 genes encoding BTB domain-containing proteins 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 BTB E3s are essential for plant development.
Volume 280(19)
Pages 18810-21
Published 2005-5-13
DOI 10.1074/jbc.M413247200
PII M413247200
PMID 15749712
MeSH Amino Acid Motifs Amino Acid Sequence Animals Arabidopsis / metabolism* Carrier Proteins / chemistry* Codon DNA / chemistry Gene Expression Regulation, Plant Heterozygote Homozygote Humans Models, Biological Molecular Sequence Data Multigene Family Mutation Oligonucleotide Array Sequence Analysis Phenotype Phylogeny Protein Binding Protein Isoforms Protein Structure, Tertiary Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Ubiquitin / chemistry Ubiquitin-Protein Ligases / chemistry*
IF 4.011
Times Cited 72
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Arabidopsis / Cultured plant cells, genes pda00987