Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity
Plant proteases are key regulators of plant cell processes such as seed development, immune responses, senescence and programmed cell death (PCD). Apoplastic papain-like cysteine proteases (PL) are hubs in plant-microbe interactions and play an important role during abiotic stresses. The apoplast is...
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doaj-69a68c306c0946c69b0d3676cfd1ec8b2020-11-25T01:16:31ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2019-04-011010.3389/fpls.2019.00473454734Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease ActivityJan Schulze Hüynck0Farnusch Kaschani1Karina van der Linde2Sebastian Ziemann3André N. Müller4Thomas Colby5Markus Kaiser6Johana C. Misas Villamil7Gunther Doehlemann8Center of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, GermanyMax Planck Institute for Plant Breeding Research, Cologne, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, GermanyCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, GermanyMax Planck Institute for Plant Breeding Research, Cologne, GermanyInstitute of Chemical Biology, University of Duisburg-Essen, Essen, GermanyCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, GermanyCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, GermanyPlant proteases are key regulators of plant cell processes such as seed development, immune responses, senescence and programmed cell death (PCD). Apoplastic papain-like cysteine proteases (PL) are hubs in plant-microbe interactions and play an important role during abiotic stresses. The apoplast is a crucial interface for the interaction between plant and microbes. So far, apoplastic maize PL and their function have been mostly described for aerial parts. In this study, we focused on apoplastic PLCPs in the roots of maize plants. We have analyzed the phylogeny of maize PLCPs and investigated their protein abundance after salicylic acid (SA) treatment. Using activity-based protein profiling (ABPP) we have identified a novel root-specific PLCP belonging to the RD21-like subfamily, as well as three SA activated PLCPs. The root specific PLCP CP1C shares sequence and structural similarities to known CP1-like proteases. Biochemical analysis of recombinant CP1C revealed different substrate specificities and inhibitor affinities compared to the related proteases. This study characterized a root-specific PLCP and identifies differences between the SA-dependent activation of PLCPs in roots and leaves.https://www.frontiersin.org/article/10.3389/fpls.2019.00473/fullrootapoplastPLCPorgan specificsalicylic acid |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jan Schulze Hüynck Farnusch Kaschani Karina van der Linde Sebastian Ziemann André N. Müller Thomas Colby Markus Kaiser Johana C. Misas Villamil Gunther Doehlemann |
spellingShingle |
Jan Schulze Hüynck Farnusch Kaschani Karina van der Linde Sebastian Ziemann André N. Müller Thomas Colby Markus Kaiser Johana C. Misas Villamil Gunther Doehlemann Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity Frontiers in Plant Science root apoplast PLCP organ specific salicylic acid |
author_facet |
Jan Schulze Hüynck Farnusch Kaschani Karina van der Linde Sebastian Ziemann André N. Müller Thomas Colby Markus Kaiser Johana C. Misas Villamil Gunther Doehlemann |
author_sort |
Jan Schulze Hüynck |
title |
Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity |
title_short |
Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity |
title_full |
Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity |
title_fullStr |
Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity |
title_full_unstemmed |
Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity |
title_sort |
proteases underground: analysis of the maize root apoplast identifies organ specific papain-like cysteine protease activity |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Plant Science |
issn |
1664-462X |
publishDate |
2019-04-01 |
description |
Plant proteases are key regulators of plant cell processes such as seed development, immune responses, senescence and programmed cell death (PCD). Apoplastic papain-like cysteine proteases (PL) are hubs in plant-microbe interactions and play an important role during abiotic stresses. The apoplast is a crucial interface for the interaction between plant and microbes. So far, apoplastic maize PL and their function have been mostly described for aerial parts. In this study, we focused on apoplastic PLCPs in the roots of maize plants. We have analyzed the phylogeny of maize PLCPs and investigated their protein abundance after salicylic acid (SA) treatment. Using activity-based protein profiling (ABPP) we have identified a novel root-specific PLCP belonging to the RD21-like subfamily, as well as three SA activated PLCPs. The root specific PLCP CP1C shares sequence and structural similarities to known CP1-like proteases. Biochemical analysis of recombinant CP1C revealed different substrate specificities and inhibitor affinities compared to the related proteases. This study characterized a root-specific PLCP and identifies differences between the SA-dependent activation of PLCPs in roots and leaves. |
topic |
root apoplast PLCP organ specific salicylic acid |
url |
https://www.frontiersin.org/article/10.3389/fpls.2019.00473/full |
work_keys_str_mv |
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