A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32

被引：1

作者：

Niu, Yulong ^{[1
]}

Xu, Xibing ^{[1
]}

Liu, Chengcheng ^{[2
]}

Wang, Tao ^{[1
]}

Liang, Ke ^{[1
]}

Wang, Jianmei ^{[1
]}

Liu, Zhibin ^{[1
]}

Li, Xufeng ^{[1
]}

Yang, Yi ^{[1
]}

机构：

[1] Sichuan Univ, Coll Life Sci, Minist Educ, Key Lab Bioresources & Ecoenvironm, Chengdu, Peoples R China

[2] Sichuan Univ, West China Hosp Stomatol, Dept Periodont, Chengdu, Peoples R China

来源：

SCIENTIFIC REPORTS | 2017年 / 7卷

关键词：

TRANSCRIPTION FACTOR SIGMA(32); STREPTOCOCCUS-MUTANS; ROSA-CHINENSIS; RICH DOMAIN; PROTEIN; INDUCTION; DNAK; GENE; RECOGNITION; EXPRESSION;

D O I：

10.1038/s41598-017-03056-6

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The heat shock response is crucial for organisms against heat-damaged proteins and maintaining homeostasis at a high temperature. Heterologous expression of eukaryotic molecular chaperones protects Escherichia coli from heat stress. Here we report that expression of the plant E3 ligase BnTR1 significantly increases the thermotolerance of E. coli. Different from eukaryotic chaperones, BnTR1 expression induces the accumulation of heat shock factor sigma(32) and heat shock proteins. The active site of BnTR1 in E. coli is the zinc fingers of the RING domain, which interacts with DnaK resulting in stabilizing s(32). Our findings indicate the expression of BnTR1 confers thermoprotective effects on E. coli cells, and it may provide useful clues to engineer thermophilic bacterial strains.

引用

页数：10

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