title: Two N-terminal acetyltransferases antagonistically regulate the stability of a nod-like receptor in Arabidopsis.
abstract: 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.
authors.affiliation: Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada.
authors.forename: Fang
authors.identifier: http://orcid.org/0000-0003-0767-1272
authors.initials: F
authors.lastname: Xu
authors.affiliation: Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada College of Life Sciences, Sichuan Agricultural University, Ya'an, Sichuan 625000, PR China.
authors.forename: Yan
authors.identifier: http://orcid.org/0000-0002-5226-2390
authors.initials: Y
authors.lastname: Huang
authors.affiliation: National Institute of Biological Sciences, Beijing 102206, PR China.
authors.forename: Lin
authors.initials: L
authors.lastname: Li
authors.affiliation: Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada.
authors.forename: Patrick
authors.initials: P
authors.lastname: Gannon
authors.affiliation: Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
authors.forename: Eric
authors.initials: E
authors.lastname: Linster
authors.affiliation: Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
authors.forename: Monika
authors.initials: M
authors.lastname: Huber
authors.affiliation: Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada.
authors.forename: Paul
authors.initials: P
authors.lastname: Kapos
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, 91198 Gif sur Yvette Cedex, France.
authors.forename: Willy
authors.initials: W
authors.lastname: Bienvenut
authors.affiliation: University of Rochester, New York 14627.
authors.forename: Bogdan
authors.identifier: http://orcid.org/0000-0002-0743-4181
authors.initials: B
authors.lastname: Polevoda
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, 91198 Gif sur Yvette Cedex, France.
authors.forename: Thierry
authors.identifier: http://orcid.org/0000-0001-5642-8637
authors.initials: T
authors.lastname: Meinnel
authors.affiliation: Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
authors.forename: Rüdiger
authors.identifier: http://orcid.org/0000-0002-6238-4818
authors.initials: R
authors.lastname: Hell
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, 91198 Gif sur Yvette Cedex, France.
authors.forename: Carmela
authors.initials: C
authors.lastname: Giglione
authors.affiliation: Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada.
authors.forename: Yuelin
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
authors.forename: Markus
authors.identifier: http://orcid.org/0000-0001-7790-4022
authors.initials: M
authors.lastname: Wirtz
authors.affiliation: National Institute of Biological Sciences, Beijing 102206, PR China.
authors.forename: She
authors.initials: S
authors.lastname: Chen
authors.affiliation: Michael Smith Laboratories, University of British Columbia, British Columbia V6T 1Z4, Canada Department of Botany, University of British Columbia, British Columbia V6T 1Z4, Canada xinli@msl.ubc.ca.
authors.forename: Xin
authors.identifier: http://orcid.org/0000-0002-6354-2021
authors.initials: X
authors.lastname: Li
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D063206:N-Terminal Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D055550:Protein Stability; D036226:Seedlings / Q000201:enzymology / Q000235:genetics; D016415:Sequence Alignment; D014026:Nicotiana / Q000201:enzymology / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; C482739:SNC1 protein, Arabidopsis; D063206:N-Terminal Acetyltransferases