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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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Publisher copy:
10.1021/acsbiomedchemau.2c00032

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
ORCID:
0000-0002-0556-1638
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
ORCID:
0000-0003-3205-7805
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author


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:
2694-2437


Language:
English
Keywords:
Pubs id:
1279533
Local pid:
pubs:1279533
Deposit date:
2022-09-22

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