Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on October 9, 2003; 10.1104/pp.103.029272

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow All Versions of this Article:
133/3/1360    most recent
pp.103.029272v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stary, S.
Right arrow Articles by Bachmair, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stary, S.
Right arrow Articles by Bachmair, A.
Agricola
Right arrow Articles by Stary, S.
Right arrow Articles by Bachmair, A.

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.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
T. Tasaki, A. Zakrzewska, D. D. Dudgeon, Y. Jiang, J. S. Lazo, and Y. T. Kwon
The Substrate Recognition Domains of the N-end Rule Pathway
J. Biol. Chem., January 16, 2009; 284(3): 1884 - 1895.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Xia, A. Webster, F. Du, K. Piatkov, M. Ghislain, and A. Varshavsky
Substrate-binding Sites of UBR1, the Ubiquitin Ligase of the N-end Rule Pathway
J. Biol. Chem., August 29, 2008; 283(35): 24011 - 24028.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
T. Tasaki, L. C. F. Mulder, A. Iwamatsu, M. J. Lee, I. V. Davydov, A. Varshavsky, M. Muesing, and Y. T. Kwon
A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons
Mol. Cell. Biol., August 15, 2005; 25(16): 7120 - 7136.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
S. L. Stone, H. Hauksdottir, A. Troy, J. Herschleb, E. Kraft, and J. Callis
Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsis
Plant Physiology, January 1, 2005; 137(1): 13 - 30.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 2003 by the American Society of Plant Biologists