SUMO Is a Critical Regulator of Salt Stress Responses in Rice

蛋白酵素 蛋白酶 水稻 相扑蛋白 生物化学 转基因水稻 转基因作物 转基因 细胞生物学 突变体 泛素 生物 基因
作者
Anjil Kumar Srivastava,Cunzin Zhang,Gary Yates,Mark Bailey,Adrian P. Brown,Ari Sadanandom
出处
期刊:Plant Physiology [Oxford University Press]
卷期号:170 (4): 2378-2391 被引量:72
标识
DOI:10.1104/pp.15.01530
摘要

SUMO (Small Ubiquitin-like Modifier) conjugation onto target proteins has emerged as a very influential class of protein modification systems. SUMO1/2 double mutant plants are nonviable, underlining the importance of SUMO conjugation to plant survival. Once covalently bound, SUMO can alter a conjugated protein's stability and/or function. SUMO conjugation is a highly dynamic process that can be rapidly reversed by the action of SUMO proteases. The balance between the conjugated/deconjugated forms is a major determinant in the modulation of SUMO-target function. Despite the important mechanistic role of SUMO proteases in model plants, until now the identity or the function of these regulatory enzymes has not been defined in any crop plant. In this report, we reveal the ubiquitin-like protease class of SUMO protease gene family in rice (Oryza sativa) and demonstrate a critical role for OsOTS1 SUMO protease in salt stress. OsOTS-RNAi rice plants accumulate high levels of SUMO-conjugated proteins during salt stress and are highly salt sensitive; however, in non-salt conditions, they are developmentally indistinguishable from wild-type plants. Transgenic rice plants overexpressing OsOTS1 have increased salt tolerance and a concomitant reduction in the levels of SUMOylated proteins. We demonstrate that OsOTS1 confers salt tolerance in rice by increasing root biomass. High salinity triggers OsOTS1 degradation, indicating that increased SUMO conjugation in rice plants during salt stress is in part achieved by down-regulation of OTS1/2 activity. OsOTS1 is nuclear localized indicating a direct requirement of OsOTS1-dependent deSUMOylation activity in rice nuclei for salt tolerance.

科研通智能强力驱动
Strongly Powered by AbleSci AI
科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
2秒前
3秒前
111发布了新的文献求助10
4秒前
互助应助炸毛胡图图采纳,获得20
4秒前
万信心发布了新的文献求助10
4秒前
依旸_Evelyn发布了新的文献求助30
5秒前
6秒前
6秒前
路痴发布了新的文献求助10
6秒前
6秒前
认真万恶完成签到,获得积分10
8秒前
万能图书馆应助dy采纳,获得10
8秒前
9秒前
Liss发布了新的文献求助10
10秒前
111发布了新的文献求助10
10秒前
11秒前
11秒前
张巨锋完成签到,获得积分10
11秒前
黑YA发布了新的文献求助10
12秒前
酷波er应助认真万恶采纳,获得10
13秒前
丹佛发布了新的文献求助10
13秒前
Dennis_Ye发布了新的文献求助10
14秒前
14秒前
华仔应助正在采纳,获得10
14秒前
打打应助吴新采纳,获得10
14秒前
15秒前
15秒前
wangying完成签到,获得积分10
15秒前
16秒前
QAQ关闭了QAQ文献求助
16秒前
16秒前
ovc发布了新的文献求助10
17秒前
18秒前
星瀚哈哈完成签到,获得积分10
18秒前
大鱼发布了新的文献求助10
19秒前
19秒前
cccxq发布了新的文献求助10
19秒前
21秒前
脑洞疼应助san采纳,获得10
22秒前
高分求助中
(应助此贴封号)【重要!!请各用户(尤其是新用户)详细阅读】【科研通的精品贴汇总】 10000
Modern Epidemiology, Fourth Edition 5000
Kinesiophobia : a new view of chronic pain behavior 5000
Molecular Biology of Cancer: Mechanisms, Targets, and Therapeutics 3000
Propeller Design 1000
Weaponeering, Fourth Edition – Two Volume SET 1000
First commercial application of ELCRES™ HTV150A film in Nichicon capacitors for AC-DC inverters: SABIC at PCIM Europe 1000
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 内科学 生物化学 物理 计算机科学 纳米技术 遗传学 基因 复合材料 化学工程 物理化学 病理 催化作用 免疫学 量子力学
热门帖子
关注 科研通微信公众号,转发送积分 6002161
求助须知:如何正确求助?哪些是违规求助? 7506156
关于积分的说明 16103584
捐赠科研通 5147071
什么是DOI,文献DOI怎么找? 2758389
邀请新用户注册赠送积分活动 1734612
关于科研通互助平台的介绍 1631202