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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Main Authors: Jan Schulze Hüynck, Farnusch Kaschani, Karina van der Linde, Sebastian Ziemann, André N. Müller, Thomas Colby, Markus Kaiser, Johana C. Misas Villamil, Gunther Doehlemann
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-04-01
Series:Frontiers in Plant Science
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fpls.2019.00473/full
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spelling 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
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