Variation in auxin sensing guides AUX/IAA transcriptional repressor ubiquitylation and destruction

Martin Winkler, Michael Niemeyer, Antje Hellmuth, Philipp Janitza, Gideon Christ, Sophia L. Samodelov, Verona Wilde, Petra Majovsky, Marco Trujillo, Matias D. Zurbriggen, Wolfgang Hoehenwarter, Marcel Quint and Luz Irina A. Calderón Villalobos ()
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Martin Winkler: Leibniz Institute of Plant Biochemistry (IPB)
Michael Niemeyer: Leibniz Institute of Plant Biochemistry (IPB)
Antje Hellmuth: Leibniz Institute of Plant Biochemistry (IPB)
Philipp Janitza: Institute of Agricultural and Nutritional Sciences, Martin Luther University Halle-Wittenberg
Gideon Christ: Leibniz Institute of Plant Biochemistry (IPB)
Sophia L. Samodelov: Institute of Synthetic Biology, University of Düsseldorf
Verona Wilde: Leibniz Institute of Plant Biochemistry (IPB)
Petra Majovsky: Proteome Analytics Research Group, Leibniz Institute of Plant Biochemistry (IPB)
Marco Trujillo: Independent Junior Research Group Ubiquitination in Immunity, Leibniz Institute of Plant Biochemistry (IPB)
Matias D. Zurbriggen: Institute of Synthetic Biology, University of Düsseldorf
Wolfgang Hoehenwarter: Proteome Analytics Research Group, Leibniz Institute of Plant Biochemistry (IPB)
Marcel Quint: Institute of Agricultural and Nutritional Sciences, Martin Luther University Halle-Wittenberg
Luz Irina A. Calderón Villalobos: Leibniz Institute of Plant Biochemistry (IPB)

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: Abstract Auxin is a small molecule morphogen that bridges SCFTIR1/AFB-AUX/IAA co-receptor interactions leading to ubiquitylation and proteasome-dependent degradation of AUX/IAA transcriptional repressors. Here, we systematically dissect auxin sensing by SCFTIR1-IAA6 and SCFTIR1-IAA19 co-receptor complexes, and assess IAA6/IAA19 ubiquitylation in vitro and IAA6/IAA19 degradation in vivo. We show that TIR1-IAA19 and TIR1-IAA6 have distinct auxin affinities that correlate with ubiquitylation and turnover dynamics of the AUX/IAA. We establish a system to track AUX/IAA ubiquitylation in IAA6 and IAA19 in vitro and show that it occurs in flexible hotspots in degron-flanking regions adorned with specific Lys residues. We propose that this signature is exploited during auxin-mediated SCFTIR1-AUX/IAA interactions. We present evidence for an evolving AUX/IAA repertoire, typified by the IAA6/IAA19 ohnologues, that discriminates the range of auxin concentrations found in plants. We postulate that the intrinsic flexibility of AUX/IAAs might bias their ubiquitylation and destruction kinetics enabling specific auxin responses.

Date: 2017
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DOI: 10.1038/ncomms15706

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