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An E3 ubiquitin ligase from Brassica napus induces a typical heat-shock response in its own way in Escherichia coil
  • ISSN号:1672-9145
  • 期刊名称:《生物化学与生物物理学报:英文版》
  • 时间:0
  • 分类:Q939.4[生物学—微生物学] S565.4[农业科学—作物学]
  • 作者机构:[1]Key Laboratory of Bio-resources and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, China, [2]CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China, [3]Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610064, China
  • 相关基金:This work was supported by the grants from the National Program on Key Basic Research Project of China (973 Project) (No. 2015CB755702 Y.Y.) and the National Natural Science Foundation of China (No. 31671455 to Y.Y.).
中文摘要:

以前,我们识别了新奇 E3 ubiquitin ligase, BNTR1,哪个戏在在 Brassica 马来麝的发情压力反应的一个关键角色。在这研究,我们偶然发现 BNTR1 能也在 42 攠灸敲獳潩 ? 景删散 ? 湩删 ? 琠獩?獥愠摮椠獴洠汯捥汵牡洠捥慨楮浳椠 ? 剅? 湩畤散 ? 灡灯潴楳? 湩删 ? 改进热忍耐和还原剂生长抑制 ?? 伭挠汥獬

英文摘要:

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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期刊信息
  • 《生物化学与生物物理学报:英文版》
  • 北大核心期刊(2004版)
  • 主管单位:
  • 主办单位:中国科学院上海生物化学研究所
  • 主编:
  • 地址:上海岳阳路319号
  • 邮编:200031
  • 邮箱:abbs@sibs.ac.cn
  • 电话:021-54920956 54920955
  • 国际标准刊号:ISSN:1672-9145
  • 国内统一刊号:ISSN:31-1940/Q
  • 邮发代号:4-210
  • 获奖情况:
  • 国内外数据库收录:
  • 美国化学文摘(网络版),英国农业与生物科学研究中心文摘,荷兰文摘与引文数据库,美国生物医学检索系统,美国剑桥科学文摘,美国科学引文索引(扩展库),美国生物科学数据库,英国动物学记录,日本日本科学技术振兴机构数据库,中国中国科技核心期刊,中国北大核心期刊(2004版),英国英国皇家化学学会文摘,中国北大核心期刊(2000版)
  • 被引量:5851