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古细菌热休克蛋白。

Archaebacterial heat-shock proteins.

机构信息

Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7.

出版信息

EMBO J. 1984 Apr;3(4):745-9. doi: 10.1002/j.1460-2075.1984.tb01878.x.

DOI:10.1002/j.1460-2075.1984.tb01878.x
PMID:16453513
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC557420/
Abstract

The response to heat shock was examined in seven archaebacterial strains from the genus Halobacterium. Upon heat shock each strain preferentially synthesized a limited number of proteins which fell into three narrow mol. wt. ranges. Further examination of the heat-shock response in H. volcanii revealed that heat-shock protein (hsp) synthesis was greatest at 60 degrees C. Synthesis of hsps at this induction temperature was both rapid and transient. Cells recovered their normal protein synthesis patterns rapidly upon returning to their normal growth temperature following heat shock. H. volcanii cells also responded with a ;heat shock-like' response to salt dilution, a natural environmental stress for these organisms. These results indicate that the heat shock or stress response which is charactertistic of eukaryotic and eubacterial cells is also present among members of the archaebacterial genus Halobacterium.

摘要

七种来自嗜盐古菌属的古细菌菌株的热休克反应被检测。热休克后,每种菌株优先合成有限数量的蛋白质,这些蛋白质分为三个狭窄的分子量范围。对嗜热古菌 H. volcanii 的热休克反应的进一步研究表明,热休克蛋白(hsp)的合成在 60°C 时最大。在这种诱导温度下,hsps 的合成既迅速又短暂。在经历热休克后回到正常生长温度时,细胞迅速恢复正常的蛋白质合成模式。嗜热古菌 H. volcanii 细胞也对盐稀释产生“热休克样”反应,这是这些生物的自然环境应激。这些结果表明,真核生物和原核生物细胞特有的热休克或应激反应也存在于嗜盐古菌属的成员中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/4b5bce0e2013/emboj00308-0061-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/0d2316195c08/emboj00308-0059-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/dafc85a07b2c/emboj00308-0059-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/81e22ec2ea21/emboj00308-0060-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/1ba6e46d6b5d/emboj00308-0060-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/b9b5eee3b01f/emboj00308-0061-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/4b5bce0e2013/emboj00308-0061-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/0d2316195c08/emboj00308-0059-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/dafc85a07b2c/emboj00308-0059-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/81e22ec2ea21/emboj00308-0060-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/1ba6e46d6b5d/emboj00308-0060-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/b9b5eee3b01f/emboj00308-0061-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c3e0/557420/4b5bce0e2013/emboj00308-0061-b.jpg

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本文引用的文献

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Can J Microbiol. 1980 Nov;26(11):1259-63. doi: 10.1139/m80-210.
2
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Mol Cell Biol. 1982 Mar;2(3):267-74. doi: 10.1128/mcb.2.3.267-274.1982.
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Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila.
热激和化学诱导伴侣蛋白基因在植物和人类细胞中的荟萃分析。
Cell Stress Chaperones. 2011 Jan;16(1):15-31. doi: 10.1007/s12192-010-0216-8. Epub 2010 Aug 9.
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Proteomic analysis of Haloferax volcanii reveals salinity-mediated regulation of the stress response protein PspA.嗜盐栖热袍菌的蛋白质组学分析揭示了盐度介导的应激反应蛋白PspA的调控。
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Genetic and transcriptomic analysis of transcription factor genes in the model halophilic Archaeon: coordinate action of TbpD and TfbA.嗜盐古菌模式生物中转录因子基因的遗传与转录组分析:TbpD和TfbA的协同作用
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Transcriptional profiling of the model Archaeon Halobacterium sp. NRC-1: responses to changes in salinity and temperature.嗜盐古菌盐沼盐杆菌NRC-1模型的转录谱分析:对盐度和温度变化的响应
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HMG-CoA reductase is regulated by salinity at the level of transcription in Haloferax volcanii.在嗜盐栖热袍菌中,HMG-CoA还原酶在转录水平受到盐度的调控。
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Intracellular localization of a group II chaperonin indicates a membrane-related function.第二组伴侣蛋白的细胞内定位表明其具有与膜相关的功能。
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