Using CRL3BPM E3 ligase substrate recognition sites as tools to impact plant development and stress tolerance in Arabidopsis thaliana

被引:3
|
作者
Al-Saharin, Raed [1 ,2 ]
Mooney, Sutton [1 ]
Dissmeyer, Nico [3 ,4 ]
Hellmann, Hanjo [1 ]
机构
[1] Washington State Univ, Pullman, WA 99164 USA
[2] Tafila Tech Univ, Tafila, Jordan
[3] Univ Osnabruck, Dept Plant Physiol, Osnabruck, Germany
[4] Univ Osnabruck, Prot Metab Lab, Osnabruck, Germany
基金
美国食品与农业研究所;
关键词
Arabidopsis; BPM; CRL3; development; E3; ligase; N-degron; stress; ubiquitin; TRANSCRIPTION FACTOR; FUNCTIONAL-ANALYSIS; PROTEINS; DEGRADATION; UBIQUITIN; COMPLEXES; DESTABILIZATION; IDENTIFICATION; EXPRESSION; WRINKLED1;
D O I
10.1002/pld3.474
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Cullin-based RING E3 ligases that use BTB/POZ-MATH (BPM) proteins as substrate receptors have been established over the last decade as critical regulators in plant development and abiotic stress tolerance. As such they affect general aspects of shoot and root development, flowering time, embryo development, and different abiotic stress responses, such as heat, drought and salt stress. To generate tools that can help to understand the role of CRL3(BPM) E3 ligases in plants, we developed a novel system using two conserved protein-binding motifs from BPM substrates to transiently block CRL3(BPM) activity. The work investigates in vitro and in planta this novel approach, and shows that it can affect stress tolerance in plants as well as developmental aspects. It thereby can serve as a new tool for studying this E3 ligase in plants.
引用
收藏
页数:14
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