Proteomics

Dataset Information

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HiRIEF TMT Proteomics of Arabidosis thaliana, wildtype versus oligopeptidases' KO mutants


ABSTRACT: Oligopeptidases Prep and OOP are enzymes located in mitochondria and chloroplasts responsible for the cleavage of long peptides (8 to 65 aas) down to short peptides (3 to 7 aas), which in turn are degraded to free amino acids by aminopeptidases such as M1 and M17. In this study, Arabidopsis thaliana knockout mutants of the genes for these enzymes were studied by proteomics using a TMT (tandem mass tags) isobaric tags quantification strategy combined with HiRIEF LC-MS on a Q-Exactive Mass Spectrometer.

INSTRUMENT(S): Q Exactive

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

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Rui Branca  

LAB HEAD: Janne Lehtiƶ

PROVIDER: PXD009651 | Pride | 2018-11-14

REPOSITORIES: Pride

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Publications

Accumulation of endogenous peptides triggers a pathogen stress response in Arabidopsis thaliana.

Kmiec Beata B   Branca Rui M M RMM   Berkowitz Oliver O   Li Lu L   Wang Yan Y   Murcha Monika W MW   Whelan James J   Lehtiƶ Janne J   Glaser Elzbieta E   Teixeira Pedro F PF  

The Plant journal : for cell and molecular biology 20181101 4


The stepwise degradation of peptides to amino acids in plant mitochondria and chloroplasts is catalyzed by a network of oligopeptidases (presequence protease PreP, organellar oligopeptidase OOP) and aminopeptidases. In the present report, we show that the lack of oligopeptidase activity in Arabidopsis thaliana results in the accumulation of endogenous free peptides, mostly of chloroplastic origin (targeting peptides and degradation products). Using mRNA sequencing and deep coverage proteomics, a  ...[more]

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