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The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity

ABSTRACT: Perception of biotic and abiotic stresses often leads to stomatal closure in plants. Rapid influx of calcium ions (Ca2+) across the plasma membrane plays an important role in this response, but the identity of Ca2+ channels involved has remained elusive. Here, we report that the Arabidopsis thaliana Ca2+-permeable channel OSCA1.3 controls stomatal closure during immunity. OSCA1.3 is rapidly phosphorylated upon perception of pathogen-associated molecular patterns (PAMPs). Biochemical and quantitative phospho-proteomics analyses reveal that the immune receptor associated cytosolic kinase BIK1 interacts with and phosphorylates the N-terminal cytosolic loop of OSCA1.3 within minutes of treatment with the peptidic PAMP flg22 derived from bacterial flagellin.

ORGANISM(S): Arabidopsis Thaliana

SUBMITTER: Frank Menke

PROVIDER: PXD020852 | panorama | Fri Sep 11 00:00:00 BST 2020

REPOSITORIES: PanoramaPublic

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The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity.

Thor Kathrin K Jiang Shushu S Michard Erwan E George Jeoffrey J Scherzer Sönke S Huang Shouguang S Dindas Julian J Derbyshire Paul P Leitão Nuno N DeFalco Thomas A TA Köster Philipp P Hunter Kerri K Kimura Sachie S Gronnier Julien J Stransfeld Lena L Kadota Yasuhiro Y Bücherl Christoph A CA Charpentier Myriam M Wrzaczek Michael M MacLean Daniel D Oldroyd Giles E D GED Menke Frank L H FLH Roelfsema M Rob G MRG Hedrich Rainer R Feijó José J Zipfel Cyril C

Nature 20200826 7826

Perception of biotic and abiotic stresses often leads to stomatal closure in plants1,2. Rapid influx of calcium ions (Ca2+) across the plasma membrane has an important role in this response, but the identity of the Ca2+ channels involved has remained elusive3,4. Here we report that the Arabidopsis thaliana Ca2+-permeable channel OSCA1.3 controls stomatal closure during immune signalling. OSCA1.3 is rapidly phosphorylated upon perception of p ...[more]

PMID: 32846426

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Project description:Many protein activities are driven by ATP binding and hydrolysis. Here, we explore the ATP binding proteome of the model plant Arabidopsis thaliana using Acyl-ATP (AcATP) probes. These probes target ATP binding sites and covalently label lysine residues in the ATP binding pocket. Protein extracts were labelled with NHS-LC-Biotin, purified over neutravidin and eluted with formic acid. Eluted proteins were separated by 1-D SDS Gel and digested with Trypsin. Peptide mixtures were analysed by LC-MS/MS on an LTQ Velos. Spectra were searched using Mascot 2.3 using a fixed modification of cysteine (57.02 Da for carbamidomethyl), and variable modifications of methionine (15.99 Da for oxidation) and lysine (339.16 and 355.16 Da for BHAc and OBHAc labeling, respectively). A mass tolerance was set to 0.3 Da for the precursor ions and 0.4 Da for fragment ions. Up to two mis-cleavages for trypsin were permitted since the labeling would prevent cleavage at the labeled lysine. The MS2 spectra were searched against the TAIR10_pep_2012 (version November 2012) containing 35386 proteins of Arabidopsis thaliana, supplemented with a small database with 1095 artefact proteins and a reversed decoy database of the same proteins (totals 72962 entries). An oxidized version of the modifier was observed. Alternatively Arabidopsis leaf proteome was labeled with desthiobiotin-acyl ATP and digested with trypsin. Labeled peptides were purified on streptavidin matrix and sequenced by LC-MS/MS on an LTQ linear ion trap. Here the MS2 spectra were searched using SEQUEST against the TAIR9_pep_20090619 database (version June 2009) containing 32,769 proteins of Arabidopsis thaliana. MS2 searches included fixed iodoacetamide modification of cysteine (57 Da for alkylation), and variable modifications of methionine (16 Da for oxidation) and lysine (196 Da for DBAcATP labeling). Up to three mis-cleavages with trypsin were allowed and non-tryptic or half-tryptic peptides were excluded. A mass tolerance was set to 3 Da for the precursor ions and 1 Da for fragment ions.

Dataset Information

The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity

Publications

The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity.

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