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    The N-end rule pathway controls multiple functions during Arabidopsis shoot and leaf development


    Graciet, Emmanuelle and Walter, Franziska and Ó’Maoiléidigh, Diarmuid S. and Pollmann, Stephan and Meyerowitz, Elliot M. and Varshavsky, Alexander and Wellmer, Frank (2009) The N-end rule pathway controls multiple functions during Arabidopsis shoot and leaf development. Proceedings of the National Academy of Sciences, 106 (32). pp. 13618-13623. ISSN 1091-6490

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    Abstract

    The ubiquitin-dependent N-end rule pathway relates the in vivo half-life of a protein to the identity of its N-terminal residue. This proteolytic system is present in all organisms examined and has been shown to have a multitude of functions in animals and fungi. In plants, however, the functional understanding of the N-end rule pathway is only beginning. The N-end rule has a hierarchic structure. Destabilizing activity of N-terminal Asp, Glu, and (oxidized) Cys requires their conjugation to Arg by an arginyl–tRNA–protein transferase (R-transferase). The resulting N-terminal Arg is recognized by the pathway’s E3 ubiquitin ligases, called ‘‘N-recognins.’’ Here, we show that the Arabidopsis R-transferases AtATE1 and AtATE2 regulate various aspects of leaf and shoot development. We also show that the previously identified N-recognin PROTEOLYSIS6 (PRT6) mediates these R-transferase-dependent activities. We further demonstrate that the arginylation branch of the N-end rule pathway plays a role in repressing the meristem-promoting BREVIPEDICELLUS (BP) gene in developing leaves. BP expression is known to be excluded from Arabidopsis leaves by the activities of the ASYMMETRIC LEAVES1 (AS1) transcription factor complex and the phytohormone auxin. Our results suggest that AtATE1 and AtATE2 act redundantly with AS1, but independently of auxin, in the control of leaf development.

    Item Type: Article
    Additional Information: This article contains supporting information online at www.pnas.org/cgi/content/full/ 0906404106/DCSupplemental.
    Keywords: arginine transferase; plant; protein degradation;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 6265
    Depositing User: Emanuelle Graciet
    Date Deposited: 17 Jul 2015 12:01
    Journal or Publication Title: Proceedings of the National Academy of Sciences
    Publisher: National Academy of Sciences
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI), National Institutes of Health, European Molecular Biology Organization, US Department of Energy
    URI:

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