通过无压缩力谱法测量GroEL与变性蛋白之间的特异性相互作用。
Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.
作者信息
Sekiguchi Hiroshi, Arakawa Hideo, Taguchi Hideki, Ito Takeshi, Kokawa Ryohei, Ikai Atsushi
机构信息
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama, Kanagawa 226-8501, Japan.
出版信息
Biophys J. 2003 Jul;85(1):484-90. doi: 10.1016/S0006-3495(03)74493-2.
Abstract
We investigated the interaction between GroEL and a denatured protein from a mechanical point of view using an atomic force microscope. Pepsin was bound to an atomic force microscope probe and used at a neutral pH as an example of denatured proteins. To measure a specific and delicate interaction force, we obtained force curves without pressing the probe onto GroEL molecules spread on a mica surface. Approximately 40 pN of tensile force was observed for approximately 10 nm while pepsin was pulled away from the chaperonin after a brief contact. This length of force duration corresponding to the circumference of GroEL's interior cavity was shortened by the addition of ATP. The relation between the observed mechanical parameters and the chaperonin's refolding function is discussed.
摘要
我们使用原子力显微镜从力学角度研究了GroEL与变性蛋白之间的相互作用。胃蛋白酶被固定在原子力显微镜探针上，并在中性pH条件下用作变性蛋白的示例。为了测量特定且微妙的相互作用力，我们在不将探针压在铺展在云母表面的GroEL分子上的情况下获得了力曲线。在短暂接触后，当胃蛋白酶从伴侣蛋白上被拉开时，在大约10纳米的距离内观察到了约40皮牛的拉力。对应于GroEL内部腔室周长的这种力持续时间长度因添加ATP而缩短。本文讨论了观察到的力学参数与伴侣蛋白的重折叠功能之间的关系。
相似文献
1
Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.通过无压缩力谱法测量GroEL与变性蛋白之间的特异性相互作用。
Biophys J. 2003 Jul;85(1):484-90. doi: 10.1016/S0006-3495(03)74493-2.
2
Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.快速扫描原子力显微镜揭示了GroEL的ATP/ADP依赖性构象变化。
EMBO J. 2006 Oct 4;25(19):4567-76. doi: 10.1038/sj.emboj.7601326. Epub 2006 Sep 14.
3
Atomic force microscopy detects changes in the interaction forces between GroEL and substrate proteins.原子力显微镜可检测GroEL与底物蛋白之间相互作用力的变化。
Biophys J. 1998 Jun;74(6):3256-63. doi: 10.1016/S0006-3495(98)78032-4.
4
Chaperonins GroEL and GroES: views from atomic force microscopy.伴侣蛋白GroEL和GroES：原子力显微镜下的观察
Biophys J. 1996 Oct;71(4):2213-21. doi: 10.1016/S0006-3495(96)79422-5.
5
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.与ATPγS复合的细菌伴侣蛋白GroEL的2.4埃晶体结构。
Nat Struct Biol. 1996 Feb;3(2):170-7. doi: 10.1038/nsb0296-170.
6
How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations.如何为原子力显微镜研究确定功能性GroEL-SR1突变体的方向。
Biochem Biophys Res Commun. 2005 Mar 11;328(2):477-83. doi: 10.1016/j.bbrc.2005.01.005.
7
Probing protein-protein interactions in real time.实时探测蛋白质-蛋白质相互作用。
Nat Struct Biol. 2000 Aug;7(8):644-7. doi: 10.1038/77936.
8
Do chaperonins boost protein yields by accelerating folding or preventing aggregation?伴侣蛋白是通过加速折叠还是防止聚集来提高蛋白质产量？
Biophys J. 2008 Apr 15;94(8):2987-93. doi: 10.1529/biophysj.107.113209. Epub 2008 Jan 11.
9
Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding.与GroEL形成蛋白质复合物的条件会影响伴侣蛋白辅助重折叠的机制。
J Biol Chem. 1997 Jan 3;272(1):32-5. doi: 10.1074/jbc.272.1.32.
10
ATP-bound states of GroEL captured by cryo-electron microscopy.通过冷冻电子显微镜捕获的GroEL的ATP结合状态。
Cell. 2001 Dec 28;107(7):869-79. doi: 10.1016/s0092-8674(01)00617-1.
引用本文的文献
1
Identification of novel protein domain for sialyloligosaccharide binding essential to Mycoplasma mobile gliding.鉴定与黏支原体滑行运动必需的唾液寡糖结合相关的新型蛋白结构域。
FEMS Microbiol Lett. 2019 Feb 1;366(3). doi: 10.1093/femsle/fnz016.
2
Nanotechnology and protein mechanics.纳米技术与蛋白质力学
J Biol Phys. 2002 Dec;28(4):561-72. doi: 10.1023/A:1021252017832.
3
Exploring the energy profile of human IgG/rat anti-human IgG interactions by dynamic force spectroscopy.通过动态力谱技术研究人 IgG/大鼠抗人 IgG 相互作用的能量特征。
Protein J. 2012 Jun;31(5):425-31. doi: 10.1007/s10930-012-9419-4.
4
Interaction between pheromone and its receptor of the fission yeast Schizosaccharomyces pombe examined by a force spectroscopy study.通过力谱学研究检测粟酒裂殖酵母信息素与其受体之间的相互作用。
J Biomed Biotechnol. 2012;2012:804793. doi: 10.1155/2012/804793. Epub 2012 Feb 21.
5
Direct detection of cellular adaptation to local cyclic stretching at the single cell level by atomic force microscopy.原子力显微镜直接检测单细胞水平对局部循环拉伸的细胞适应性。
Biophys J. 2011 Feb 2;100(3):564-572. doi: 10.1016/j.bpj.2010.12.3693.
6
Nanobiomechanics of proteins and biomembrane.蛋白质与生物膜的纳米生物力学
Philos Trans R Soc Lond B Biol Sci. 2008 Jun 27;363(1500):2163-71. doi: 10.1098/rstb.2008.2269.
7
mRNA detection of individual cells with the single cell nanoprobe method compared with in situ hybridization.单细胞纳米探针法与原位杂交法检测单个细胞的 mRNA。
J Nanobiotechnology. 2007 Oct 10;5:7. doi: 10.1186/1477-3155-5-7.
8
Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.快速扫描原子力显微镜揭示了GroEL的ATP/ADP依赖性构象变化。
EMBO J. 2006 Oct 4;25(19):4567-76. doi: 10.1038/sj.emboj.7601326. Epub 2006 Sep 14.
本文引用的文献
1
Dual function of protein confinement in chaperonin-assisted protein folding.伴侣蛋白辅助蛋白质折叠中蛋白质受限的双重功能。
Cell. 2001 Oct 19;107(2):223-33. doi: 10.1016/s0092-8674(01)00517-7.
2
Probing protein-protein interactions in real time.实时探测蛋白质-蛋白质相互作用。
Nat Struct Biol. 2000 Aug;7(8):644-7. doi: 10.1038/77936.
3
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.蛋白酶体对大部分新合成蛋白质的快速降解。
Nature. 2000 Apr 13;404(6779):770-4. doi: 10.1038/35008096.
4
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.伴侣蛋白GroEL对非天然底物蛋白的多价结合
Cell. 2000 Mar 3;100(5):561-73. doi: 10.1016/s0092-8674(00)80692-3.
5
Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.GroEL顶端结构域的亲水性残基有助于GroES结合，但会减弱多肽结合。
Biochem Biophys Res Commun. 2000 Jan 27;267(3):842-9. doi: 10.1006/bbrc.1999.2020.
6
Posttranslational quality control: folding, refolding, and degrading proteins.翻译后质量控制：蛋白质的折叠、重折叠及降解
Science. 1999 Dec 3;286(5446):1888-93. doi: 10.1126/science.286.5446.1888.
7
GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.GroEL可加速溶菌酶的重折叠过程，而不改变其折叠机制。
Nat Struct Biol. 1999 Jul;6(7):683-90. doi: 10.1038/10735.
8
GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings.GroEL - GroES循环：ATP和非天然多肽引导折叠活性环的交替。
Cell. 1999 Apr 30;97(3):325-38. doi: 10.1016/s0092-8674(00)80742-4.
9
Spatially resolved force spectroscopy of biological surfaces using the atomic force microscope.使用原子力显微镜对生物表面进行空间分辨力谱分析。
Trends Biotechnol. 1999 Apr;17(4):143-50. doi: 10.1016/s0167-7799(99)01304-9.
10
Structure and function in GroEL-mediated protein folding.GroEL介导的蛋白质折叠中的结构与功能
Annu Rev Biochem. 1998;67:581-608. doi: 10.1146/annurev.biochem.67.1.581.
Zotero 插件