Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis

T. Sato; S. Maekawa; S. Yasuda; Y. Domeki; K. Sueyoshi; M. Fujiwara; Y. Fukao; D.B. Goto; J. Yamaguchi

doi:10.1111/j.1365-313X.2011.04673.x

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Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis

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Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis

T. Sato, S. Maekawa, S. Yasuda, Y. Domeki, K. Sueyoshi, M. Fujiwara, Y. Fukao, D.B. Goto and J. Yamaguchi

The Plant Journal, Vol.68(1), pp.137-146

2011

DOI: https://doi.org/10.1111/j.1365-313X.2011.04673.x

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Abstract

The balance between carbon (C) and nitrogen (N) availability is an important determinant for various phases of plant growth; however, the detailed mechanisms regulating the C/N response are not well understood. We previously described two related ubiquitin ligases, ATL31 and ATL6, that function in the C/N response in Arabidopsis thaliana. Here, we used FLAG tag affinity purification and MS analysis to identify proteins targeted by ATL31, and thus likely to be involved in regulating the phase transition checkpoint based on C/N status. This analysis revealed that 14-3-3 proteins were associated with ATL31, and one of these, 14-3-3π, was selected for detailed characterization. The interaction between ATL31 and 14-3-3π was confirmed by yeast two-hybrid and co-immunoprecipitation analyses. In vitro assays showed that ubiquitination of 14-3-3π is catalyzed by ATL31. Degradation of 14-3-3πin vivo was shown to be correlated with ATL31 activity, and to occur in a proteasome-dependent manner. Furthermore, 14-3-3 protein accumulation was induced by a shift to high-C/N stress conditions in Arabidopsis seedlings, and this regulated response required both ATL31 and ATL6. It was also shown that over-expression of 14-3-3π leads to hypersensitivity of Arabidopsis seedlings to C/N stress conditions. These results indicate that ATL31 targets and ubiquitinates 14-3-3 proteins for degradation via the ubiquitin-proteasome system during the response to cellular C/N status.

Details

Title: Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis
Authors/Creators: T. Sato (Author/Creator) - Hokkaido University
S. Maekawa (Author/Creator) - Hokkaido University
S. Yasuda (Author/Creator) - Hokkaido University
Y. Domeki (Author/Creator) - Hokkaido University
K. Sueyoshi (Author/Creator) - Niigata University
M. Fujiwara (Author/Creator) - Nara Institute of Science and Technology
Y. Fukao (Author/Creator) - Nara Institute of Science and Technology
D.B. Goto (Author/Creator) - Hokkaido University
J. Yamaguchi (Author/Creator) - Hokkaido University
Publication Details: The Plant Journal, Vol.68(1), pp.137-146
Publisher: Blackwell Publishing
Identifiers: 991005540809307891
Copyright: © 2011 Blackwell Publishing Ltd.
Murdoch Affiliation: Murdoch University
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration
Citation topics: 3 Agriculture, Environment & Ecology; 3.4 Crop Science; 3.4.1209 Plant Sugar Metabolism
Web Of Science research areas: Plant Sciences
ESI research areas: Plant & Animal Science