Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae
All aerobic organisms require O2 for survival. When their O2 is limited (hypoxia), a response is required to reduce demand and/or improve supply. A hypoxic response mechanism has been identified in flowering plants: the stability of certain proteins with N-terminal cysteine residues is regulated in...
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Materiálatiipa: | Journal article |
Giella: | English |
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American Chemical Society
2022
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author | Taylor-Kearney, LJ Madden, S Wilson, J Myers, WK Gunawardana, DM Pires, E Holdship, P Tumber, A Rickaby, REM Tumber, A Flashman, E |
author_facet | Taylor-Kearney, LJ Madden, S Wilson, J Myers, WK Gunawardana, DM Pires, E Holdship, P Tumber, A Rickaby, REM Tumber, A Flashman, E |
author_sort | Taylor-Kearney, LJ |
collection | OXFORD |
description | All aerobic organisms require O2 for survival. When their O2 is limited (hypoxia), a response is required to reduce demand and/or improve supply. A hypoxic response mechanism has been identified in flowering plants: the stability of certain proteins with N-terminal cysteine residues is regulated in an O2-dependent manner by the Cys/Arg branch of the N-degron pathway. These include the Group VII ethylene response factors (ERF-VIIs), which can initiate adaptive responses to hypoxia. Oxidation of their N-terminal cysteine residues is catalyzed by plant cysteine oxidases (PCOs), destabilizing these proteins in normoxia; PCO inactivity in hypoxia results in their stabilization. Biochemically, the PCOs are sensitive to O2 availability and can therefore act as plant O2 sensors. It is not known whether oxygen-sensing mechanisms exist in other phyla from the plant kingdom. Known PCO targets are only conserved in flowering plants, however PCO-like sequences appear to be conserved in all plant species. We sought to determine whether PCO-like enzymes from the liverwort, Marchantia polymorpha (MpPCO), and the freshwater algae, Klebsormidium nitens (KnPCO), have a similar function as PCO enzymes from Arabidopsis thaliana. We report that MpPCO and KnPCO show O2-sensitive N-terminal cysteine dioxygenase activity toward known AtPCO ERF-VII substrates as well as a putative endogenous substrate, MpERF-like, which was identified by homology to the Arabidopsis ERF-VIIs transcription factors. This work confirms functional and O2-dependent PCOs from Bryophyta and Charophyta, indicating the potential for PCO-mediated O2-sensing pathways in these organisms and suggesting PCO O2-sensing function could be important throughout the plant kingdom. |
first_indexed | 2024-03-07T08:09:21Z |
format | Journal article |
id | oxford-uuid:41d75dfe-054e-41d1-a8eb-7c53fdfcd848 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T08:09:21Z |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | dspace |
spelling | oxford-uuid:41d75dfe-054e-41d1-a8eb-7c53fdfcd8482023-11-17T15:40:42ZPlant cysteine oxidase oxygen-sensing function is conserved in early land plants and algaeJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:41d75dfe-054e-41d1-a8eb-7c53fdfcd848EnglishSymplectic ElementsAmerican Chemical Society2022Taylor-Kearney, LJMadden, SWilson, JMyers, WKGunawardana, DMPires, EHoldship, PTumber, ARickaby, REMTumber, AFlashman, EAll aerobic organisms require O2 for survival. When their O2 is limited (hypoxia), a response is required to reduce demand and/or improve supply. A hypoxic response mechanism has been identified in flowering plants: the stability of certain proteins with N-terminal cysteine residues is regulated in an O2-dependent manner by the Cys/Arg branch of the N-degron pathway. These include the Group VII ethylene response factors (ERF-VIIs), which can initiate adaptive responses to hypoxia. Oxidation of their N-terminal cysteine residues is catalyzed by plant cysteine oxidases (PCOs), destabilizing these proteins in normoxia; PCO inactivity in hypoxia results in their stabilization. Biochemically, the PCOs are sensitive to O2 availability and can therefore act as plant O2 sensors. It is not known whether oxygen-sensing mechanisms exist in other phyla from the plant kingdom. Known PCO targets are only conserved in flowering plants, however PCO-like sequences appear to be conserved in all plant species. We sought to determine whether PCO-like enzymes from the liverwort, Marchantia polymorpha (MpPCO), and the freshwater algae, Klebsormidium nitens (KnPCO), have a similar function as PCO enzymes from Arabidopsis thaliana. We report that MpPCO and KnPCO show O2-sensitive N-terminal cysteine dioxygenase activity toward known AtPCO ERF-VII substrates as well as a putative endogenous substrate, MpERF-like, which was identified by homology to the Arabidopsis ERF-VIIs transcription factors. This work confirms functional and O2-dependent PCOs from Bryophyta and Charophyta, indicating the potential for PCO-mediated O2-sensing pathways in these organisms and suggesting PCO O2-sensing function could be important throughout the plant kingdom. |
spellingShingle | Taylor-Kearney, LJ Madden, S Wilson, J Myers, WK Gunawardana, DM Pires, E Holdship, P Tumber, A Rickaby, REM Tumber, A Flashman, E Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title | Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title_full | Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title_fullStr | Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title_full_unstemmed | Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title_short | Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae |
title_sort | plant cysteine oxidase oxygen sensing function is conserved in early land plants and algae |
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