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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.<\/jats:p>","DOI":"10.1104\/pp.103.029272","type":"journal-article","created":{"date-parts":[[2003,11,11]],"date-time":"2003-11-11T23:33:05Z","timestamp":1068593585000},"page":"1360-1366","source":"Crossref","is-referenced-by-count":72,"title":["PRT1 of Arabidopsis Is a Ubiquitin Protein Ligase of the Plant N-End Rule Pathway with Specificity for Aromatic Amino-Terminal Residues"],"prefix":"10.1093","volume":"133","author":[{"given":"Susanne","family":"Stary","sequence":"first","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]},{"given":"Xiao-jun","family":"Yin","sequence":"additional","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]},{"given":"Thomas","family":"Potuschak","sequence":"additional","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]},{"given":"Peter","family":"Schlo\u0308gelhofer","sequence":"additional","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]},{"given":"Victoria","family":"Nizhynska","sequence":"additional","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]},{"given":"Andreas","family":"Bachmair","sequence":"additional","affiliation":[{"name":"Institute of Botany, University of Vienna, Rennweg 14, A\u20131030 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\u201350829 Cologne, Germany (X.-j.Y., A.B.)"}]}],"member":"286","published-online":{"date-parts":[[2003,11,11]]},"reference":[{"key":"2021042910263255200_REF1","doi-asserted-by":"crossref","unstructured":"Anderson TJ, Robers RP, Jarrett HW (1996) Ca2+-Calmodulin binds to the carboxyl-terminal domain of dystrophin. 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