Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway
Citations Over TimeTop 1% of 2014 papers
Abstract
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.
Related Papers
- → Mammalian Cysteine Metabolism: New Insights into Regulation of Cysteine Metabolism(2006)534 cited
- → Inhibition of the alternative oxidase stimulates H2O2 production in plant mitochondria(1997)174 cited
- → Cysteine Concentration Regulates Cysteine Metabolism to Glutathione, Sulfate and Taurine in Rat Hepatocytes(1992)163 cited
- → Induction and activation of cysteine oxidase of rat liver II. The measurement of cysteine metabolism in vivo and the activation of in vivo activity of cysteine oxidase(1973)98 cited
- → Metabolism of Cysteine, Cysteinesulfinate and Cysteinesulfonate in Rats Fed Adequate and Excess Levels of Sulfur-Containing Amino Acids(1984)40 cited