An E3 ubiquitin ligase from Brassica napus induces a typical heat-shock response in its own way in Escherichia coil
Previously, we have identified a novel E3 ubiquitin ligase, BNTR1, which plays a key role in heat stress response in Brassica napus. In this study, we accidentally found that BNTR1 can also improve thermal tolerance and reduce growth inhibition at 42℃ in Escherichia coli, in a manner different from...
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Published in | 生物化学与生物物理学报:英文版 Vol. 49; no. 3; pp. 262 - 269 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
2017
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Subjects | |
Online Access | Get full text |
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Summary: | Previously, we have identified a novel E3 ubiquitin ligase, BNTR1, which plays a key role in heat stress response in Brassica napus. In this study, we accidentally found that BNTR1 can also improve thermal tolerance and reduce growth inhibition at 42℃ in Escherichia coli, in a manner different from that in plant. We show that BNTR1 activates E. coil heat-shock response at low concentration in soluble form instead of in inclusion body, but BNTR1 is not functioning as a heat- shock protein (HSP) because deficient temperature-sensitive mutants of HSP genes display un- conspicuous thermal tolerance in the presence of BNTRI. Our further studies show that BNTR1 triggers heat-shock response by competing with σ32 (σ32, heat-shock transcription factor) to its binding proteins DnaJ (HSP40) and DnaK (HSP70), which results in the release and accumulation of σ32, thereby promoting the heat-shock response, even under the non-heat-shock conditions. At 37℃, accumulation of the HSPs induced by BNTR1 could make cells much more tolerant than those without BNTR1 at 42℃. Thus, our results suggest that BNTR1 may potentially be a promis- ing target in fermentation industry for reducing impact from temperature fluctuation, where E. coli works as bioreactors. |
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Bibliography: | 31-1940/Q Previously, we have identified a novel E3 ubiquitin ligase, BNTR1, which plays a key role in heat stress response in Brassica napus. In this study, we accidentally found that BNTR1 can also improve thermal tolerance and reduce growth inhibition at 42℃ in Escherichia coli, in a manner different from that in plant. We show that BNTR1 activates E. coil heat-shock response at low concentration in soluble form instead of in inclusion body, but BNTR1 is not functioning as a heat- shock protein (HSP) because deficient temperature-sensitive mutants of HSP genes display un- conspicuous thermal tolerance in the presence of BNTRI. Our further studies show that BNTR1 triggers heat-shock response by competing with σ32 (σ32, heat-shock transcription factor) to its binding proteins DnaJ (HSP40) and DnaK (HSP70), which results in the release and accumulation of σ32, thereby promoting the heat-shock response, even under the non-heat-shock conditions. At 37℃, accumulation of the HSPs induced by BNTR1 could make cells much more tolerant than those without BNTR1 at 42℃. Thus, our results suggest that BNTR1 may potentially be a promis- ing target in fermentation industry for reducing impact from temperature fluctuation, where E. coli works as bioreactors. E3 ubiquitin ligase, heat-shock response,σ32, thermal resistance |
ISSN: | 1672-9145 1745-7270 |