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1
The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.细菌热休克蛋白ClpB/HSP100的截短形式有助于蓝藻聚球藻属PCC 7942菌株耐热性的形成。
J Bacteriol. 2000 Dec;182(24):7092-6. doi: 10.1128/JB.182.24.7092-7096.2000.
2
The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.热休克蛋白ClpB介导了聚球藻属蓝细菌PCC 7942菌株耐热性的形成。
J Bacteriol. 1996 Aug;178(16):4839-46. doi: 10.1128/jb.178.16.4839-4846.1996.
3
Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942.热休克蛋白ClpB的诱导影响了聚球藻属蓝细菌PCC 7942菌株的冷驯化。
J Bacteriol. 1997 Aug;179(16):5111-7. doi: 10.1128/jb.179.16.5111-5117.1997.
4
The Escherichia coli heat shock protein ClpB restores acquired thermotolerance to a cyanobacterial clpB deletion mutant.大肠杆菌热休克蛋白ClpB可恢复蓝藻clpB缺失突变体的获得性耐热性。
Cell Stress Chaperones. 2000 Jul;5(3):255-64. doi: 10.1379/1466-1268(2000)005<0255:techsp>2.0.co;2.
5
Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus.蓝藻聚球藻中ClpB/HSP100蛋白的新形式。
J Bacteriol. 2001 Dec;183(24):7392-6. doi: 10.1128/JB.183.24.7392-7396.2001.
6
The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli DeltaclpB mutant cells--new insight into the role of Hsp70 in a functional cooperation with Hsp100.DnaK/DnaJ/GrpE和ClpB蛋白共同过量表达对从大肠杆菌DeltaclpB突变体细胞中去除热聚集蛋白的影响——对Hsp70与Hsp100功能协同作用中作用的新见解。
FEMS Microbiol Lett. 2001 Nov 13;204(2):355-60. doi: 10.1111/j.1574-6968.2001.tb10910.x.
7
Acquired thermotolerance and expression of the HSP100/ClpB genes of lima bean.利马豆的获得性耐热性及HSP100/ClpB基因的表达
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8
ClpB/Hsp100 proteins and heat stress tolerance in plants.ClpB/Hsp100 蛋白与植物的热应激耐性。
Crit Rev Biotechnol. 2016 Oct;36(5):862-74. doi: 10.3109/07388551.2015.1051942. Epub 2015 Jun 30.
9
The involvement of chloroplast HSP100/ClpB in the acquired thermotolerance in tomato.叶绿体HSP100/ClpB参与番茄的获得性耐热性。
Plant Mol Biol. 2006 Oct;62(3):385-95. doi: 10.1007/s11103-006-9027-9. Epub 2006 Aug 16.
10
Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system.遗传分析揭示了拟南芥Hsp100/ClpB的结构域相互作用及其与小分子热激蛋白伴侣系统的协同作用。
Plant Cell. 2005 Feb;17(2):559-71. doi: 10.1105/tpc.104.027540. Epub 2005 Jan 19.

引用本文的文献

1
Ultrafast pore-loop dynamics in a AAA+ machine point to a Brownian-ratchet mechanism for protein translocation.AAA+ 机器中超快的孔环动力学指向蛋白质转运的布朗棘轮机制。
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Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.结核分枝杆菌 ClpB-DnaK 双伴侣蛋白系统介导聚集物溶解和重折叠的结构基础。
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Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain.熵抑制：AAA+ 机器的活性如何被其底物结合域调节。
ACS Chem Biol. 2021 Apr 16;16(4):775-785. doi: 10.1021/acschembio.1c00156. Epub 2021 Mar 19.
4
The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity.ClpB蛋白的氨基末端结构域在其底物解聚活性中起关键作用。
FEBS Open Bio. 2018 Sep 15;8(10):1669-1690. doi: 10.1002/2211-5463.12509. eCollection 2018 Oct.
5
Adaptive laboratory evolution of cadmium tolerance in sp. PCC 6803.聚球藻属PCC 6803对镉耐受性的适应性实验室进化
Biotechnol Biofuels. 2018 Jul 24;11:205. doi: 10.1186/s13068-018-1205-x. eCollection 2018.
6
Genes within Genes in Bacterial Genomes.细菌基因组中的基因内基因。
Microbiol Spectr. 2018 Jul;6(4). doi: 10.1128/microbiolspec.RWR-0020-2018.
7
Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria.独立的 ClpG 解聚酶赋予细菌更高的耐热性。
Proc Natl Acad Sci U S A. 2018 Jan 9;115(2):E273-E282. doi: 10.1073/pnas.1712051115. Epub 2017 Dec 20.
8
Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.Hsp104 N 结构域的重叠和特定功能决定了其在蛋白质解聚中的作用。
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9
Identification of a Halotolerant Mutant via In Vitro Mutagenesis in the Cyanobacterium Fremyella diplosiphon.通过对蓝藻双岐鱼腥藻进行体外诱变鉴定出一株耐盐突变体。
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10
Molecular chaperones: guardians of the proteome in normal and disease states.分子伴侣：正常及疾病状态下蛋白质组的守护者
F1000Res. 2015 Dec 15;4. doi: 10.12688/f1000research.7214.1. eCollection 2015.

本文引用的文献

1
The Escherichia coli heat shock protein ClpB restores acquired thermotolerance to a cyanobacterial clpB deletion mutant.大肠杆菌热休克蛋白ClpB可恢复蓝藻clpB缺失突变体的获得性耐热性。
Cell Stress Chaperones. 2000 Jul;5(3):255-64. doi: 10.1379/1466-1268(2000)005<0255:techsp>2.0.co;2.
2
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.热不稳定大肠杆菌蛋白的鉴定：DnaK和ClpB对聚集的预防及逆转作用
EMBO J. 1999 Dec 15;18(24):6934-49. doi: 10.1093/emboj/18.24.6934.
3
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.双分子伴侣网络对稳定蛋白质聚集体进行溶解和重折叠的顺序机制
Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13732-7. doi: 10.1073/pnas.96.24.13732.
4
ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli.ClpB与DnaK、DnaJ和GrpE协同作用以抑制蛋白质聚集。一种来自大肠杆菌的新型多分子伴侣系统。
J Biol Chem. 1999 Oct 1;274(40):28083-6. doi: 10.1074/jbc.274.40.28083.
5
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones.热失活蛋白可被DnaK.J-GrpE复合物和ClpB伴侣蛋白拯救。
Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7184-9. doi: 10.1073/pnas.96.13.7184.
6
Lon and Clp family proteases and chaperones share homologous substrate-recognition domains.Lon蛋白酶和Clp家族蛋白酶及伴侣蛋白共享同源的底物识别结构域。
Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6678-82. doi: 10.1073/pnas.96.12.6678.
7
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.热休克蛋白104、热休克蛋白70和热休克蛋白40：一种拯救先前聚集蛋白的新型伴侣系统。
Cell. 1998 Jul 10;94(1):73-82. doi: 10.1016/s0092-8674(00)81223-4.
8
Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942.热休克蛋白ClpB的诱导影响了聚球藻属蓝细菌PCC 7942菌株的冷驯化。
J Bacteriol. 1997 Aug;179(16):5111-7. doi: 10.1128/jb.179.16.5111-5117.1997.
9
The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.分子伴侣Hsp78赋予线粒体特定区室的耐热性。
J Cell Biol. 1996 Sep;134(6):1375-86. doi: 10.1083/jcb.134.6.1375.
10
HSP100/Clp proteins: a common mechanism explains diverse functions.热休克蛋白100/Clp蛋白：一种共同机制解释多种功能。
Trends Biochem Sci. 1996 Aug;21(8):289-96.

细菌热休克蛋白ClpB/HSP100的截短形式有助于蓝藻聚球藻属PCC 7942菌株耐热性的形成。

The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.

作者信息

Clarke A K, Eriksson M J

机构信息

Umeå Plant Sciences Centre, Department of Plant Physiology, University of Umeâ, Umeâ S-901 87, Sweden.

出版信息

J Bacteriol. 2000 Dec;182(24):7092-6. doi: 10.1128/JB.182.24.7092-7096.2000.

DOI:10.1128/JB.182.24.7092-7096.2000
PMID:11092876
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC94841/
Abstract

ClpB is a highly conserved heat shock protein that is essential for thermotolerance in bacteria and eukaryotes. One distinctive feature of all bacterial clpB genes is the dual translation of a truncated 79-kDa form (ClpB-79) in addition to the full-length 93-kDa protein (ClpB-93). To investigate the currently unknown function of ClpB-79, we have examined the ability of the two different-sized ClpB homologues from the cyanobacterium Synechococcus sp. strain PCC 7942 to confer thermotolerance. We show that the ClpB-79 form has the same capacity as ClpB-93 to confer thermotolerance and that the ClpB-79 protein contributes ca. one-third of the total thermotolerance developed in wild-type Synechococcus, the first in vivo demonstration of a functional role for ClpB-79 in bacteria.

摘要

ClpB是一种高度保守的热休克蛋白，对细菌和真核生物的耐热性至关重要。所有细菌clpB基因的一个显著特征是，除了全长93 kDa的蛋白质（ClpB-93）外，还会双重翻译出截短的79 kDa形式（ClpB-79）。为了研究目前未知的ClpB-79的功能，我们检测了来自蓝藻聚球藻属PCC 7942菌株的两种不同大小的ClpB同源物赋予耐热性的能力。我们发现，ClpB-79形式与ClpB-93具有相同的赋予耐热性的能力，并且ClpB-79蛋白对野生型聚球藻产生的总耐热性贡献约三分之一，这是首次在体内证明ClpB-79在细菌中的功能作用。