期刊
JOURNAL OF INTEGRATIVE PLANT BIOLOGY
卷 62, 期 1, 页码 70-89出版社
WILEY
DOI: 10.1111/jipb.12882
关键词
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资金
- Biotechnology and Biological Sciences Research Council [BB/R002428/1, BB/M029441/1]
- Leverhulme Trust Research Project [RPG-2017-132, RPG-2018-172]
- University of Nottingham joint Biosciences/Chemistry Ph.D. fellowship
- BBSRC [BB/R002428/1, BB/M029441/1] Funding Source: UKRI
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.
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