A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32
Abstract 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 BnTR...
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Nature Portfolio
2017
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oai:doaj.org-article:ecc2883457aa4e63b817f314909fe81f2021-12-02T12:32:27ZA novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ3210.1038/s41598-017-03056-62045-2322https://doaj.org/article/ecc2883457aa4e63b817f314909fe81f2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03056-6https://doaj.org/toc/2045-2322Abstract 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 σ32 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 σ32. 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.Yulong NiuXibing XuChengcheng LiuTao WangKe LiangJianmei WangZhibin LiuXufeng LiYi YangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017) |
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EN |
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Medicine R Science Q |
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Medicine R Science Q Yulong Niu Xibing Xu Chengcheng Liu Tao Wang Ke Liang Jianmei Wang Zhibin Liu Xufeng Li Yi Yang A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| description |
Abstract 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 σ32 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 σ32. 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. |
| format |
article |
| author |
Yulong Niu Xibing Xu Chengcheng Liu Tao Wang Ke Liang Jianmei Wang Zhibin Liu Xufeng Li Yi Yang |
| author_facet |
Yulong Niu Xibing Xu Chengcheng Liu Tao Wang Ke Liang Jianmei Wang Zhibin Liu Xufeng Li Yi Yang |
| author_sort |
Yulong Niu |
| title |
A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| title_short |
A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| title_full |
A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| title_fullStr |
A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| title_full_unstemmed |
A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σ32 |
| title_sort |
novel plant e3 ligase stabilizes escherichia coli heat shock factor σ32 |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/ecc2883457aa4e63b817f314909fe81f |
| work_keys_str_mv |
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