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Plant Physiol, December 2000, Vol. 124, pp. 1828-1843
The Ubiquitin-Specific Protease Family from Arabidopsis.
AtUBP1 and 2 Are Required for the
Resistance to the Amino Acid Analog Canavanine1
Ning
Yan,2
Jed H.
Doelling,
Tanya G.
Falbel,3
Adam M.
Durski, and
Richard D.
Vierstra*
Cellular and Molecular Biology Program and the Department of
Horticulture, University of Wisconsin, Madison, Wisconsin 53706
Ubiquitin-specific proteases (UBPs) are a family of unique
hydrolases that specifically remove polypeptides covalently linked via
peptide or isopeptide bonds to the C-terminal glycine of ubiquitin. UBPs help regulate the ubiquitin/26S proteolytic pathway by generating free ubiquitin monomers from their initial translational products, recycling ubiquitins during the breakdown of ubiquitin-protein conjugates, and/or by removing ubiquitin from specific targets and thus
presumably preventing target degradation. Here, we describe a family of
27 UBP genes from Arabidopsis that contain both the conserved cysteine (Cys) and histidine boxes essential for catalysis. They can be clustered into 14 subfamilies based on sequence similarity, genomic organization, and alignments with their closest relatives from
other organisms, with seven subfamilies having two or more members.
Recombinant AtUBP2 functions as a bona fide UBP: It can release polypeptides attached to ubiquitins via either  - or
 -amino linkages by an activity that requires the predicted
active-site Cys within the Cys box. From the analysis of T-DNA
insertion mutants, we demonstrate that the AtUBP1 and
2 subfamily helps confer resistance to the arginine
analog canavanine. This phenotype suggests that the
AtUBP1 and 2 enzymes are needed for abnormal protein
turnover in Arabidopsis.
1
This work was supported by the U.S. Department
of Agriculture-National Research Initiative Competitive Grants Program
(grant nos. 97-35301-4218 and 00-35301-9040) and the Research
Division of the University of Wisconsin, College of Agriculture and
Life Sciences (grant no. Hatch 142-N936), a National Institutes of Health Postdoctoral Fellowship (to J.H.D.), and a U.S. Department of
Agriculture Postdoctoral Grant (to T.G.F.).
2
Present address: Department of Biochemistry, University
of Washington, Seattle, WA 98195.
3
Present address: Department of Biochemistry, University
of Wisconsin, Madison, WI 53706.
*
Corresponding author; e-mail vierstra{at}facstaff.wisc.edu; fax
608-262-4743.
© 2000 American Society of Plant Physiologists
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