The plant N‐degron pathways of ubiquitin‐mediated proteolysis. Issue 1 (21st December 2019)
- Record Type:
- Journal Article
- Title:
- The plant N‐degron pathways of ubiquitin‐mediated proteolysis. Issue 1 (21st December 2019)
- Main Title:
- The plant N‐degron pathways of ubiquitin‐mediated proteolysis
- Authors:
- Holdsworth, Michael John
Vicente, Jorge
Sharma, Gunjan
Abbas, Mohamad
Zubrycka, Agata - Editors:
- Gong, Zhizhong
- Abstract:
- Abstract : Selective destruction of proteins is a key point of regulation for intracellular homeostasis. Here we review the plant N‐degron pathways of ubiquitin‐mediated proteolysis, which target proteins through the recognition of aminoterminal residue. These pathways control multiple important aspects of development and stress responses, including the sensing of oxygen and nitric oxide. Abstract: The amino‐terminal residue of a protein (or amino‐terminus of a peptide following protease cleavage) can be an important determinant of its stability, through the Ubiquitin Proteasome System associated N‐degron pathways. Plants contain a unique combination of N‐degron pathways (previously called the N‐end rule pathways) E3 ligases, PROTEOLYSIS (PRT)6 and PRT1, recognizing non‐overlapping sets of amino‐terminal residues, and others remain to be identified. Although only very few substrates of PRT1 or PRT6 have been identified, substrates of the oxygen and nitric oxide sensing branch of the PRT6 N‐degron pathway include key nuclear‐located transcription factors (ETHYLENE RESPONSE FACTOR VIIs and LITTLE ZIPPER 2) and the histone‐modifying Polycomb Repressive Complex 2 component VERNALIZATION 2. In response to reduced oxygen or nitric oxide levels (and other mechanisms that reduce pathway activity) these stabilized substrates regulate diverse aspects of growth and development, including response to flooding, salinity, vernalization (cold‐induced flowering) and shoot apical meristemAbstract : Selective destruction of proteins is a key point of regulation for intracellular homeostasis. Here we review the plant N‐degron pathways of ubiquitin‐mediated proteolysis, which target proteins through the recognition of aminoterminal residue. These pathways control multiple important aspects of development and stress responses, including the sensing of oxygen and nitric oxide. Abstract: The amino‐terminal residue of a protein (or amino‐terminus of a peptide following protease cleavage) can be an important determinant of its stability, through the Ubiquitin Proteasome System associated N‐degron pathways. Plants contain a unique combination of N‐degron pathways (previously called the N‐end rule pathways) E3 ligases, PROTEOLYSIS (PRT)6 and PRT1, recognizing non‐overlapping sets of amino‐terminal residues, and others remain to be identified. Although only very few substrates of PRT1 or PRT6 have been identified, substrates of the oxygen and nitric oxide sensing branch of the PRT6 N‐degron pathway include key nuclear‐located transcription factors (ETHYLENE RESPONSE FACTOR VIIs and LITTLE ZIPPER 2) and the histone‐modifying Polycomb Repressive Complex 2 component VERNALIZATION 2. In response to reduced oxygen or nitric oxide levels (and other mechanisms that reduce pathway activity) these stabilized substrates regulate diverse aspects of growth and development, including response to flooding, salinity, vernalization (cold‐induced flowering) and shoot apical meristem function. The N‐degron pathways show great promise for use in the improvement of crop performance and for biotechnological applications. Upstream proteases, components of the different pathways and associated substrates still remain to be identified and characterized to fully appreciate how regulation of protein stability through the amino‐terminal residue impacts plant biology. … (more)
- Is Part Of:
- Journal of integrative plant biology. Volume 62:Issue 1(2020)
- Journal:
- Journal of integrative plant biology
- Issue:
- Volume 62:Issue 1(2020)
- Issue Display:
- Volume 62, Issue 1 (2020)
- Year:
- 2020
- Volume:
- 62
- Issue:
- 1
- Issue Sort Value:
- 2020-0062-0001-0000
- Page Start:
- 70
- Page End:
- 89
- Publication Date:
- 2019-12-21
- Subjects:
- Plants -- Periodicals
Plants -- China -- Periodicals
Electronic journals
580.5 - Journal URLs:
- http://bibpurl.oclc.org/web/10380 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1744-7909 ↗
http://www.blackwell-synergy.com/loi/jipb ↗
http://www.blackwell-synergy.com/openurl?genre=journal&eissn=1744-7909 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/jipb.12882 ↗
- Languages:
- English
- ISSNs:
- 1672-9072
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5007.538427
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 12663.xml