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Two N-Terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in arabidopsis

Nod-like receptors (NLRs) serve as immune receptors in plants and animals. The stability of NLRs is tightly regulated, though its mechanism is not well understood. Here, we show the crucial impact of N-terminal acetylation on the turnover of one plant NLR, Suppressor of NPR1, Constitutive 1 (SNC1),...

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Bibliographic Details
Main Authors: Xu, Fang (Author) , Linster, Eric (Author) , Huber, Monika (Author) , Hell, Rüdiger (Author) , Wirtz, Markus (Author)
Format: Article (Journal)
Language:English
Published: May 12, 2015
In: The plant cell
Year: 2015, Volume: 27, Issue: 5, Pages: 1547-1562
ISSN:1532-298X
DOI:10.1105/tpc.15.00173
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1105/tpc.15.00173
Verlag, kostenfrei, Volltext: http://www.plantcell.org/content/27/5/1547
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Author Notes:Fang Xu, Yan Huang, Lin Li, Patrick Gannon, Eric Linster, Monika Huber, Paul Kapos, Willy Bienvenut, Bogdan Polevoda, Thierry Meinnel, Rüdiger Hell, Carmela Giglione, Yuelin Zhang, Markus Wirtz, She Chen, and Xin Li
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Summary:Nod-like receptors (NLRs) serve as immune receptors in plants and animals. The stability of NLRs is tightly regulated, though its mechanism is not well understood. Here, we show the crucial impact of N-terminal acetylation on the turnover of one plant NLR, Suppressor of NPR1, Constitutive 1 (SNC1), in Arabidopsis thaliana. Genetic and biochemical analyses of SNC1 uncovered its multilayered regulation by different N-terminal acetyltransferase (Nat) complexes. SNC1 exhibits a few distinct N-terminal isoforms generated through alternative initiation and N-terminal acetylation. Its first Met is acetylated by N-terminal acetyltransferase complex A (NatA), while the second Met is acetylated by N-terminal acetyltransferase complex B (NatB). Unexpectedly, the NatA-mediated acetylation serves as a degradation signal, while NatB-mediated acetylation stabilizes the NLR protein, thus revealing antagonistic N-terminal acetylation of a single protein substrate. Moreover, NatA also contributes to the turnover of another NLR, RESISTANCE TO P. syringae pv maculicola 1. The intricate regulation of protein stability by Nats is speculated to provide flexibility for the target protein in maintaining its homeostasis.
Item Description:Gesehen am 17.05.2017
Physical Description:Online Resource
ISSN:1532-298X
DOI:10.1105/tpc.15.00173

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