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拟南芥E3 SUMO连接酶AtSIZ1的翻译后修饰受环境条件控制。

Post-translational modifications of Arabidopsis E3 SUMO ligase AtSIZ1 are controlled by environmental conditions.

作者信息

Kim Joo Yong, Song Jong Tae, Seo Hak Soo

机构信息

Department of Plant ScienceResearch Institute for Agriculture and Life Sciences, and Plant Genomics and Breeding InstituteSeoul National UniversityKorea.

School of Applied BiosciencesKyungpook National UniversityDaeguKorea.

出版信息

FEBS Open Bio. 2017 Sep 18;7(10):1622-1634. doi: 10.1002/2211-5463.12309. eCollection 2017 Oct.

DOI:10.1002/2211-5463.12309
PMID:28979848
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5623694/
Abstract

Sumoylation regulates numerous cellular functions in plants as well as in other eukaryotic systems. However, the regulatory mechanisms controlling E3 small ubiquitin-related modifier (SUMO) ligase are not well understood. Here, post-translational modification of the Arabidopsis E3 SUMO ligase AtSIZ1 was shown to be specifically controlled by abiotic stresses. AtSIZ1 ubiquitination was induced by exposure to heat stress in transgenic plants overexpressing the E3 ubiquitin ligase COP1. In addition, AtSIZ1 ubiquitination was strongly enhanced in transgenic plants overexpressing SUMO isopeptidase ESD4 under heat stress. By contrast, drought stress induced sumoylation rather than ubiquitination of AtSIZ1 and sumoylated forms of AtSIZ1 accumulated in and mutants. Moreover, mutants were found to be tolerant to heat and drought stresses. Taken together, these results indicate that ubiquitination and sumoylation of AtSIZ1 in response to abiotic stresses depend on the activities of COP1 and ESD4 and that the activity and stability of AtSIZ1 can be specifically controlled by different abiotic stresses.

摘要

SUMO化修饰在植物以及其他真核生物系统中调控着众多细胞功能。然而,控制E3小泛素相关修饰物(SUMO)连接酶的调控机制尚未完全明晰。在此,拟南芥E3 SUMO连接酶AtSIZ1的翻译后修饰被证明受到非生物胁迫的特异性调控。在过表达E3泛素连接酶COP1的转基因植物中,热胁迫诱导了AtSIZ1的泛素化。此外,在热胁迫下,过表达SUMO异肽酶ESD4的转基因植物中AtSIZ1的泛素化显著增强。相比之下,干旱胁迫诱导了AtSIZ1的SUMO化修饰而非泛素化修饰,并且AtSIZ1的SUMO化形式在 和 突变体中积累。此外,发现 突变体对热胁迫和干旱胁迫具有耐受性。综上所述,这些结果表明,AtSIZ1在响应非生物胁迫时的泛素化和SUMO化修饰依赖于COP1和ESD4的活性,并且AtSIZ1的活性和稳定性可受到不同非生物胁迫的特异性调控。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/88aeb8f8b39b/FEB4-7-1622-g007.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/00dafd9a496a/FEB4-7-1622-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/dbc9549755ec/FEB4-7-1622-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/88aeb8f8b39b/FEB4-7-1622-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/5d894a559009/FEB4-7-1622-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/b305e4266aa1/FEB4-7-1622-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/3e87afe93725/FEB4-7-1622-g003.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/00dafd9a496a/FEB4-7-1622-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/5623694/dbc9549755ec/FEB4-7-1622-g006.jpg
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