Author
Listed:
- Martin Winkler
(Leibniz Institute of Plant Biochemistry (IPB)
Present address: Institute of Biochemistry, ETH Zurich, Zurich 8093, Switzerland)
- 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
Spemann Graduate School of Biology and Medicine (SGBM), University of Freiburg)
- 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
Cluster of Excellence on Plant Science (CEPLAS), 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))
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.
Suggested Citation
Martin Winkler & Michael Niemeyer & Antje Hellmuth & Philipp Janitza & Gideon Christ & Sophia L. Samodelov & Verona Wilde & Petra Majovsky & Marco Trujillo & Matias D. Zurbriggen & Wolfgang Hoehenwart, 2017.
"Variation in auxin sensing guides AUX/IAA transcriptional repressor ubiquitylation and destruction,"
Nature Communications, Nature, vol. 8(1), pages 1-13, August.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15706
DOI: 10.1038/ncomms15706
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