Proteomics

Dataset Information

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Moss secreted peptidome - Salicylic acid influences the protease activity and posttranslation modifications of the secreted peptides in the moss Physcomitrella patens


ABSTRACT: Plant secretome comprise dozens of secreted proteins and peptide hormones. However, little is known about peptide composition of plant secretome as well as proteases responsible for peptide pools generation. While the majority of studies focuses on the target detection and characterization of specific plant peptide hormones, we performed a comprehensive analysis of the whole extracellular peptidome, using moss Physcomitrella patens as a model object. We identified hundreds of modified and unmodified endogenous peptides originated from functional and non-functional protein precursors. Plant proteases responsible for shaping the pool of endogenous peptides were predicted. We showed that salicylic acid (SA) induces peptide production in the secretome.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Physcomitrella Patens Subsp. Patens (moss)

TISSUE(S): Plant Cell, Cell Culture

SUBMITTER: Igor Fesenko  

LAB HEAD: Vadim Govorun

PROVIDER: PXD010964 | Pride | 2019-01-02

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
SA-1.zip Other
SA-2.zip Other
SA-3.zip Other
SA-4.zip Other
control-1.zip Other
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Publications

Salicylic acid influences the protease activity and posttranslation modifications of the secreted peptides in the moss Physcomitrella patens.

Filippova Anna A   Lyapina Irina I   Kirov Ilya I   Zgoda Victor V   Belogurov Alexey A   Kudriaeva Anna A   Ivanov Vadim V   Fesenko Igor I  

Journal of peptide science : an official publication of the European Peptide Society 20181221 2


Plant secretome comprises dozens of secreted proteins. However, little is known about the composition of the whole secreted peptide pools and the proteases responsible for the generation of the peptide pools. The majority of studies focus on target detection and characterization of specific plant peptide hormones. In this study, we performed a comprehensive analysis of the whole extracellular peptidome, using moss Physcomitrella patens as a model. Hundreds of modified and unmodified endogenous p  ...[more]

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