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Nipped in the bud: a microbial effector destabilizes MADS-domain transcription factors

ABSTRACT: Eluates from pull down experiments were separated on an SDS gel, and bands isolated for in gel trypsin digestion. Digested samples were analysed by LCMSMS on an Orbitrap. Peaklists were generated using MaxQuant 1.3.0.5 and database searches performed using Mascot Server 2.4. Data from all gel slices from one sample were merged in one Mascot search, and the results were imported into Scaffold 4.0.4.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Gerhard Saalbach

LAB HEAD: Gerhard Saalbach

PROVIDER: PXD000223 | Pride | 2014-05-21

REPOSITORIES: Pride

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			Action	DRS
	130402_03.raw	Raw
	130402_04.raw	Raw
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	130402_07.raw	Raw

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Publications

Phytoplasma effector SAP54 hijacks plant reproduction by degrading MADS-box proteins and promotes insect colonization in a RAD23-dependent manner.

MacLean Allyson M AM Orlovskis Zigmunds Z Kowitwanich Krissana K Zdziarska Anna M AM Angenent Gerco C GC Immink Richard G H RG Hogenhout Saskia A SA

PLoS biology 20140408 4

Pathogens that rely upon multiple hosts to complete their life cycles often modify behavior and development of these hosts to coerce them into improving pathogen fitness. However, few studies describe mechanisms underlying host coercion. In this study, we elucidate the mechanism by which an insect-transmitted pathogen of plants alters floral development to convert flowers into vegetative tissues. We find that phytoplasma produce a novel effector protein (SAP54) that interacts with members of the ...[more]

PMID: 24714165

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Arabidopsis cell LC-MSMS - Proteomics analysis reveals a highly heterogeneous proteasome composition and the post-translational regulation of peptidase activity under pathogen signaling in plants

Project description:26S proteasome was affinity-purified with anti-FLAG beads and separated by 2-DE method. Each spot was cut and digested by Trypsin enzyme, which finaly applied for LC-MS/MS nalysis using a LTQ-Orbitrap XL (Thermo Scientific). The obtained spectra were compared against 35,386 sequences in The Arabidopsis Information Resource 10 (TAIR10; http://www.arabidopsis.org/) using the MASCOT server (version 2.4; Matrix Science) with the following search parameters: threshold set-off at 0.05 in the ion-score cut-off; protein identification cut-off set to two assigned spectra per predicted protein; peptide tolerance at 10 ppm; MS/MS tolerance at +/- 0.5 Da; peptide charge of 2+ or 3+; trypsin as the enzyme and allowing up to one missed cleavage; carboxymethylation on cysteines as a fixed modification and oxidation on methionine as a variable modification.

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Proteome-wide purification of O-GlcNAc proteins

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