Journal article
Plant cysteine oxidase oxygen-sensing function is conserved in early land plants and algae
- Abstract:
- 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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 3.4MB, Terms of use)
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- Publisher copy:
- 10.1021/acsbiomedchemau.2c00032
Authors
- Publisher:
- American Chemical Society
- Journal:
- ACS Bio & Med Chem Au More from this journal
- Volume:
- 2
- Issue:
- 5
- Pages:
- 521–528
- Publication date:
- 2022-08-15
- Acceptance date:
- 2022-07-27
- DOI:
- EISSN:
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2694-2437
- Language:
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English
- Keywords:
- Pubs id:
-
1279533
- Local pid:
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pubs:1279533
- Deposit date:
-
2022-09-22
Terms of use
- Copyright holder:
- Taylor-Kearney et al.
- Copyright date:
- 2022
- Rights statement:
- © 2022 The Authors. Published by American Chemical Society. This paper is made open access via Creative Commons licensing (https://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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