Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway

Daan A. Weits, Beatrice Giuntoli, Monika Kosmacz, Sandro Parlanti, Hans Michael Hubberten, Heike Riegler, Rainer Hoefgen, Pierdomenico Perata, Joost T. Van Dongen, Francesco Licausi

Research output: Contribution to journalArticlepeer-review

266 Scopus citations


In plant and animal cells, amino-terminal cysteine oxidation controls selective proteolysis via an oxygen-dependent branch of the N-end rule pathway. It remains unknown how the N-terminal cysteine is specifically oxidized. Here we identify plant cysteine oxidase (PCO) enzymes that oxidize the penultimate cysteine of ERF-VII transcription factors by using oxygen as a co-substrate, thereby controlling the lifetime of these proteins. Consequently, ERF-VII proteins are stabilized under hypoxia and activate the molecular response to low oxygen while the expression of anaerobic genes is repressed in air. Members of the PCO family are themselves targets of ERF-VII transcription factors, generating a feedback loop that adapts the stress response according to the extent of the hypoxic condition. Our results reveal that PCOs act as sensor proteins for oxygen in plants and provide an example of how proactive regulation of the N-end rule pathway balances stress response to optimal growth and development in plants. © 2014 Macmillan Publishers Limited. All rights reserved.
Original languageEnglish (US)
JournalNature Communications
StatePublished - Mar 6 2014
Externally publishedYes

Bibliographical note

Generated from Scopus record by KAUST IRTS on 2021-02-18


Dive into the research topics of 'Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway'. Together they form a unique fingerprint.

Cite this