Proteomics

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Protein abundance and phosphorylation changes in feronia mutant arabidopsis rosette leaves


ABSTRACT: The goal of this study was to determine protein abundance and phosphorylation changes in the FERONIA mutant (fer) in Arabidopsis leaves. Seeds were germinated on 1/2MS with constant light (24hr light) for 10 days. Then, plants were transferred to soil and grown under short day condition (8-hour light and 16-hour dark) at 22C for another 3 weeks (21 days). Samples were 4 weeks old when collected. Three biological replicates of WT as well as fer mutant rosette leaves were collected at 4 weeks. Proteins were extracted and processed into peptides using a phenol-FASP methods (https://doi.org/10.1002/pmic.201800220). Peptides were labeled with TMT6-plex reagents (WT 126, 127N, 128C; fer 129N, 130C, 131). Following TMT multiplexing phoshopeptides were enriched using Titanspere Phos-TiO 10 uM beads (GL science).

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Justin Walley  

PROVIDER: MSV000084804 | MassIVE | Tue Jan 14 12:09:00 GMT 2020

REPOSITORIES: MassIVE

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The receptor kinase FERONIA (FER) is a versatile regulator of plant growth and development, biotic and abiotic stress responses, and reproduction. To gain new insights into the molecular interplay of these processes and to identify new FER functions, we carried out quantitative transcriptome, proteome, and phosphoproteome profiling of Arabidopsis (Arabidopsis thaliana) wild-type and fer-4 loss-of-function mutant plants. Gene ontology terms for phytohormone signaling, abiotic stress, and biotic s  ...[more]

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