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泛素特异性蛋白酶 UBP12 和 UBP13 通过增强 PIF7 的稳定性来促进避荫反应。

Ubiquitin-specific proteases UBP12 and UBP13 promote shade avoidance response by enhancing PIF7 stability.

机构信息

Temasek Life Sciences Laboratory, National University of Singapore, Singapore 117604.

Disruptive & Sustainable Technologies for Agricultural Precision, Singapore-MIT Alliance for Research and Technology, Singapore 138602.

出版信息

Proc Natl Acad Sci U S A. 2021 Nov 9;118(45). doi: 10.1073/pnas.2103633118.

Abstract

Changes in light quality caused by the presence of neighbor proximity regulate many growth and development processes of plants. PHYTOCHROME INTERACTING FACTOR 7 (PIF7), whose subcellular localization, DNA-binding properties, and protein abundance are regulated in a photoreversible manner, plays a central role in linking shade light perception and growth responses. How PIF7 activity is regulated during shade avoidance responses has been well studied, and many factors involved in this process have been identified. However, the detailed molecular mechanism by which shade light regulates the PIF7 protein level is still largely unknown. Here, we show that the PIF7 protein level regulation is important for shade-induced growth. Two ubiquitin-specific proteases, UBP12 and UBP13, were identified as positive regulators in shade avoidance responses by increasing the PIF7 protein level. The - double mutant displayed significantly impaired sensitivity to shade-induced cell elongation and reproduction acceleration. Our genetic and biochemical analysis showed that UBP12 and UBP13 act downstream of phyB and directly interact with PIF7 to maintain PIF7 stability and abundance through deubiquitination.

摘要

邻近效应引起的光质变化调控着植物的许多生长和发育过程。光形态建成素互作因子 7(PIF7)的亚细胞定位、DNA 结合特性和蛋白丰度以光可逆的方式调控,在连接荫蔽光感知和生长反应中起着核心作用。PIF7 活性在避荫反应中是如何被调控的已经得到了很好的研究,并且已经鉴定出许多参与这个过程的因素。然而,荫蔽光调控 PIF7 蛋白水平的详细分子机制在很大程度上仍然未知。在这里,我们表明 PIF7 蛋白水平的调控对于荫蔽诱导的生长是重要的。两个泛素特异性蛋白酶,UBP12 和 UBP13,通过增加 PIF7 蛋白水平被鉴定为避荫反应中的正调控因子。ubp12 和 ubp13 的双突变体显示出对荫蔽诱导的细胞伸长和繁殖加速的敏感性显著降低。我们的遗传和生化分析表明,UBP12 和 UBP13 作为 phyB 的下游因子发挥作用,通过去泛素化作用直接与 PIF7 相互作用,从而维持 PIF7 的稳定性和丰度。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b577/8609341/72762803c94e/pnas.202103633fig01.jpg

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