噬菌体Mu的头部和尾部组装在大肠杆菌groEL和groES突变体中受阻。
Assembly of both the head and tail of bacteriophage Mu is blocked in Escherichia coli groEL and groES mutants.
作者信息
Grimaud R, Toussaint A
机构信息
Unité Transposition Bactérienne, Université Libre de Bruxelles, Rhode St Genèse, Belgium.
出版信息
J Bacteriol. 1998 Mar;180(5):1148-53. doi: 10.1128/JB.180.5.1148-1153.1998.
Abstract
Like several other Escherichia coli bacteriophages, transposable phage Mu does not develop normally in groE hosts (M. Pato, M. Banerjee, L. Desmet, and A. Toussaint, J. Bacteriol. 169:5504-5509, 1987). We show here that lysates obtained upon induction of groE Mu lysogens contain free inactive tails and empty heads. GroEL and GroES are thus essential for the correct assembly of both Mu heads and Mu tails. Evidence is presented that groE mutations inhibit processing of the phage head protein gpH as well as the formation of a 25S complex suspected to be an early Mu head assembly intermediate.
摘要
与其他几种大肠杆菌噬菌体一样，可转座噬菌体Mu在groE宿主中不能正常发育（M. 帕托、M. 班纳吉、L. 德梅特和A. 图桑，《细菌学杂志》169:5504 - 5509, 1987年）。我们在此表明，诱导groE Mu溶原菌后获得的裂解物含有游离的无活性尾部和空头部。因此，GroEL和GroES对于Mu头部和Mu尾部的正确组装至关重要。有证据表明，groE突变会抑制噬菌体头部蛋白gpH的加工以及一种疑似早期Mu头部组装中间体的25S复合物的形成。
相似文献
1
Assembly of both the head and tail of bacteriophage Mu is blocked in Escherichia coli groEL and groES mutants.噬菌体Mu的头部和尾部组装在大肠杆菌groEL和groES突变体中受阻。
J Bacteriol. 1998 Mar;180(5):1148-53. doi: 10.1128/JB.180.5.1148-1153.1998.
2
Assembly of membrane-containing bacteriophage PRD1 is dependent on GroEL and GroES.含膜噬菌体PRD1的组装依赖于GroEL和GroES。
Virology. 1997 Jan 6;227(1):207-10. doi: 10.1006/viro.1996.8308.
3
Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer.利用荧光能量共振转移研究 GroEL-gp31 分子伴侣复合物的离解动力学。
Biochemistry. 2009 Dec 15;48(49):11692-8. doi: 10.1021/bi9013962.
4
Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.伴侣蛋白GroEL/GroES的共表达增强了酵母线粒体乌头酸酶的体内折叠，并改变了大肠杆菌的生长特性。
Int J Biochem Cell Biol. 2006;38(11):1975-85. doi: 10.1016/j.biocel.2006.05.013. Epub 2006 Jun 2.
5
Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli.两类基因外抑制突变鉴定出了大肠杆菌GroEL伴侣蛋白功能上不同的区域。
J Bacteriol. 1994 Nov;176(21):6558-65. doi: 10.1128/jb.176.21.6558-6565.1994.
6
Cloning and characterization of the groE heat-shock operon of the marine bacterium Vibrio harveyi.哈维氏弧菌groE热休克操纵子的克隆与特性分析
Microbiology (Reading). 2003 Jun;149(Pt 6):1483-1492. doi: 10.1099/mic.0.26273-0.
7
Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.有效的ATP酶活性和适度的伴侣蛋白-共伴侣蛋白相互作用对于功能性单环伴侣蛋白系统很重要。
Biochem Biophys Res Commun. 2015 Oct 9;466(1):15-20. doi: 10.1016/j.bbrc.2015.08.034. Epub 2015 Aug 11.
8
Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.噬菌体T4编码一种共伴侣蛋白，它在蛋白质折叠过程中可替代大肠杆菌的GroES。
Nature. 1994 Apr 14;368(6472):654-6. doi: 10.1038/368654a0.
9
An ORFan no more: the bacteriophage T4 39.2 gene product, NwgI, modulates GroEL chaperone function.不再是孤儿：噬菌体 T4 的 39.2 基因产物 NwgI 调节 GroEL 伴侣蛋白功能。
Genetics. 2012 Mar;190(3):989-1000. doi: 10.1534/genetics.111.135640. Epub 2012 Jan 10.
10
Stable expression and rapid purification of Escherichia coli GroEL and GroES chaperonins.大肠杆菌GroEL和GroES伴侣蛋白的稳定表达与快速纯化。
Protein Expr Purif. 1997 Oct;11(1):47-52. doi: 10.1006/prep.1997.0764.
引用本文的文献
1
Genomic and Proteomic Characterization of Bacteriophage BH1 Spontaneously Released from Probiotic Pen.从益生菌 Pen 中自发释放的噬菌体 BH1 的基因组和蛋白质组特征
Viruses. 2019 Dec 16;11(12):1163. doi: 10.3390/v11121163.
2
Novel chaperonins are prevalent in the virioplankton and demonstrate links to viral biology and ecology.新型伴侣蛋白在浮游病毒群落中普遍存在，并显示出与病毒生物学和生态学的联系。
ISME J. 2017 Nov;11(11):2479-2491. doi: 10.1038/ismej.2017.102. Epub 2017 Jul 21.
本文引用的文献
1
Sensitive mutants of bacteriophage lambda.噬菌体λ的敏感突变体
Virology. 1961 May;14:22-32. doi: 10.1016/0042-6822(61)90128-3.
2
In vivo observation of polypeptide flux through the bacterial chaperonin system.通过细菌伴侣蛋白系统对多肽通量的体内观察。
Cell. 1997 Aug 8;90(3):491-500. doi: 10.1016/s0092-8674(00)80509-7.
3
Bacteriophage Mu head assembly.
Virology. 1996 Mar 1;217(1):200-10. doi: 10.1006/viro.1996.0107.
4
Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.细菌胞质蛋白在体内的折叠：GroEL的作用
Cell. 1993 Sep 10;74(5):909-17. doi: 10.1016/0092-8674(93)90470-b.
5
Molecular chaperone functions of heat-shock proteins.热休克蛋白的分子伴侣功能
Annu Rev Biochem. 1993;62:349-84. doi: 10.1146/annurev.bi.62.070193.002025.
6
Characterization of a functionally important mobile domain of GroES.GroES功能重要的可移动结构域的表征
Nature. 1993 Jul 15;364(6434):255-8. doi: 10.1038/364255a0.
7
Sequence analysis and phenotypic characterization of groEL mutations that block lambda and T4 bacteriophage growth.阻断λ噬菌体和T4噬菌体生长的groEL基因突变的序列分析及表型特征
J Bacteriol. 1993 Feb;175(4):1134-43. doi: 10.1128/jb.175.4.1134-1143.1993.
8
Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding.多肽与分子伴侣的相互作用及其与体内蛋白质折叠的关系。
Annu Rev Biophys Biomol Struct. 1994;23:645-69. doi: 10.1146/annurev.bb.23.060194.003241.
9
Complexes between chaperonin GroEL and the capsid protein of bacteriophage HK97.
Biochemistry. 1995 Nov 14;34(45):14918-31. doi: 10.1021/bi00045a037.
10
Assembly in vitro of bacteriophage HK97 proheads.噬菌体HK97原头部的体外组装
J Mol Biol. 1995 Oct 13;253(1):74-85. doi: 10.1006/jmbi.1995.0537.
Zotero 插件