ProPlantStress

Proteolytic processing in plant stress signal transduction and responses to abiotic stress and pathogen attack

CoordinatorForschungszentrum Jülich
Grant period2015-06-01 - 2020-11-30
Funding bodyEuropean Union
Call numberERC-2014-STG
Grant number639905
IdentifierG:(EU-Grant)639905

Note: Site-specific proteolytic processing is an irreversible post-translational protein modification that generates distinct protein species with new functions, interactions and subcellular locations. In plants, proteolytic processing regulates hormonal and stress signaling leading to adaptation of metabolic pathways and is implicated in plant-pathogen interactions. Despite their importance, proteolytic processes have largely been identified serendipitously, specific cleavage sites have rarely been identified and only a few of the hundreds of proteases encoded in plant genomes (>800 in Arabidopsis) have been linked to any substrates. Positional proteomics enables system-wide identification of proteolytic processing and protease substrate repertoires through quantitative determination of protein N- or C-termini. ProPlantStress will employ these approaches, which I co-developed during my postdoctoral research, to two linked abiotic and biotic stress conditions: i) Time-resolved mapping of chloroplast protein processing induced by high intensity light will reveal novel mechanisms of retrograde signal transduction, stress response and acclimation; ii) Profiling of protein processing triggered by pathogen recognition, combined with substrate identification for selected host and bacterial pathogen effector proteases will identify proteins with novel functions in plant immune responses and systemic signaling. Importantly, ProPlantStress will not merely catalogue termini and substrates: Mapping of cleavage sites to the protein domains and correlation with other modifications, such as phosphorylation, generates testable hypotheses on the function of processed protein species that will be examined in detail. ProPlantStress will thereby provide fundamental insights into proteolytic mechanisms underlying plant stress responses that are unattainable by other means. In the long term such knowledge is needed to develop new strategies for crop protection and mitigation of harvest loss.
     

Recent Publications

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The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities
ACS catalysis 11(19), 11885 - 11896 () [10.1021/acscatal.1c02057] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Cutting the line: manipulation of plant immunity by bacterial type III effector proteases
The journal of experimental botany 72(9), 3395 - 3409 () [10.1093/jxb/erab095] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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MANTI: Automated Annotation of Protein N-Termini for Rapid Interpretation of N-Terminome Data Sets
Analytical chemistry 93(13), 5596–5605 () [10.1021/acs.analchem.1c00310] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Abundance of metalloprotease FtsH12 modulates chloroplast development in Arabidopsis thaliana
The journal of experimental botany 72(9), 3455–3473 () [10.1093/jxb/eraa550] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Structural and functional studies of Arabidopsis thaliana legumain beta reveal isoform specific mechanisms of activation and substrate recognition
The journal of biological chemistry 295, 13047-13064 () [10.1074/jbc.RA120.014478] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Photoprotective Acclimation of the Arabidopsis thaliana Leaf Proteome to Fluctuating Light
Frontiers in genetics 11, 154 () [10.3389/fgene.2020.00154] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease
Analytical chemistry 92(4), 2961-2971 () [10.1021/acs.analchem.9b03604] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Sensitive determination of proteolytic proteoforms in limited microscale proteome samples
Molecular & cellular proteomics 18(11), 2335-2347 () [10.1074/mcp.TIR119.001560] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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DEG10 contributes to mitochondrial proteostasis, root growth and seed yield in Arabidopsis
The journal of experimental botany 70(19), 5423–5436 () [10.1093/jxb/erz294] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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A fungal substrate mimicking molecule suppresses plant immunity via an inter-kingdom conserved motif
Nature Communications 10(1), 1576 () [10.1038/s41467-019-09472-8] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

All known publications ...
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 Record created 2015-09-13, last modified 2023-02-10



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