Oxygen-dependent proteolysis regulates the stability of angiosperm polycomb repressive complex 2 subunit VERNALIZATION 2. Issue 1 (December 2018)
- Record Type:
- Journal Article
- Title:
- Oxygen-dependent proteolysis regulates the stability of angiosperm polycomb repressive complex 2 subunit VERNALIZATION 2. Issue 1 (December 2018)
- Main Title:
- Oxygen-dependent proteolysis regulates the stability of angiosperm polycomb repressive complex 2 subunit VERNALIZATION 2
- Authors:
- Gibbs, Daniel
Tedds, Hannah
Labandera, Anne-Marie
Bailey, Mark
White, Mark
Hartman, Sjon
Sprigg, Colleen
Mogg, Sophie
Osborne, Rory
Dambire, Charlene
Boeckx, Tinne
Paling, Zachary
Voesenek, Laurentius
Flashman, Emily
Holdsworth, Michael - Abstract:
- Abstract The polycomb repressive complex 2 (PRC2) regulates epigenetic gene repression in eukaryotes. Mechanisms controlling its developmental specificity and signal-responsiveness are poorly understood. Here, we identify an oxygen-sensitive N-terminal (N-) degron in the plant PRC2 subunit VERNALIZATION(VRN) 2, a homolog of animal Su(z)12, that promotes its degradation via the N-end rule pathway. We provide evidence that this N-degron arose early during angiosperm evolution via gene duplication and N-terminal truncation, facilitating expansion of PRC2 function in flowering plants. We show that proteolysis via the N-end rule pathway prevents ectopic VRN2 accumulation, and that hypoxia and long-term cold exposure lead to increased VRN2 abundance, which we propose may be due to inhibition of VRN2 turnover via its N-degron. Furthermore, we identify an overlap in the transcriptional responses to hypoxia and prolonged cold, and show that VRN2 promotes tolerance to hypoxia. Our work reveals a mechanism for post-translational regulation of VRN2 stability that could potentially link environmental inputs to the epigenetic control of plant development. VRN2 is a Polycomb Repressive Complex 2 subunit, best known as a regulator of vernalization that accumulates during prolonged cold. Here Gibbset al . show that VRN2 is degraded via the N-end rule pathway, which prevents ectopic accumulation of VRN2 in the absence of appropriate environmental stimuli.
- Is Part Of:
- Nature communications. Volume 9:Issue 1(2018)
- Journal:
- Nature communications
- Issue:
- Volume 9:Issue 1(2018)
- Issue Display:
- Volume 9, Issue 1 (2018)
- Year:
- 2018
- Volume:
- 9
- Issue:
- 1
- Issue Sort Value:
- 2018-0009-0001-0000
- Page Start:
- 1
- Page End:
- 11
- Publication Date:
- 2018-12
- Subjects:
- Biology -- Periodicals
Physical sciences -- Periodicals
505 - Journal URLs:
- http://www.nature.com/ncomms/index.html ↗
http://www.nature.com/ ↗ - DOI:
- 10.1038/s41467-018-07875-7 ↗
- Languages:
- English
- ISSNs:
- 2041-1723
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6046.280270
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12707.xml