Plant Physiology Preview
Published on October 9, 2003; 10.1104/pp.103.029272
Received June 29, 2003
Returned for revision July 16, 2003
Accepted July 21, 2003
PRT1 of Arabidopsis Is a Ubiquitin Protein Ligase of the Plant N-End Rule Pathway with Specificity for Aromatic Amino-Terminal Residues
Susanne Stary , Xiao-jun Yin , Thomas Potuschak , Peter Schlögelhofer , Victoria Nizhynska , and Andreas Bachmair *
Institute of Botany, University of Vienna, Rennweg 14, A-1030 Vienna, Austria (S.S., T.P., P.S., V.N., A.B.); and Max Planck Institute for Plant Breeding Research, Department of Plant Developmental Biology, D-50829 Cologne, Germany (X.-j.Y., A.B.)
* Corresponding author; email: bachmair{at}mpiz-koeln.mpg.de.
The gene PRT1 of Arabidopsis, encoding a 45-kD protein with two RING finger domains, is essential for the degradation of F-dihydrofolate reductase, a model substrate of the N-end rule pathway of protein degradation. We have determined the function of PRT1 by expression in yeast (Saccharomyces cerevisiae). PRT1 can act as a ubiquitin protein ligase in the heterologous host. The identified substrates of PRT1 have an aromatic residue at their amino-terminus, indicating that PRT1 mediates degradation of N-end rule substrates with aromatic termini but not of those with aliphatic or basic amino-termini. Expression of model substrates in mutant and wild-type plants confirmed this substrate specificity. A ligase activity exclusively devoted to aromatic amino-termini of the N-end rule pathway is apparently unique to plants. The results presented also imply that other known substrates of the plant N-end rule pathway are ubiquitylated by one or more different ubiquitin protein ligases.
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