静电相互作用对驱动蛋白马达运动的影响

doi:10.3969/j.issn.1000-1565.2017.03.003

河北大学学报(自然科学版) ›› 2017, Vol. 37 ›› Issue (3): 237-242.DOI: 10.3969/j.issn.1000-1565.2017.03.003

静电相互作用对驱动蛋白马达运动的影响

黄艳宾¹,郭海军¹,李洁²,刘秀红¹,纪青³

收稿日期:2016-12-10 出版日期:2017-05-25 发布日期:2017-05-25
作者简介:黄艳宾(1981—),男,河北邯郸人,河北工程大学讲师,主要从事分子马达和大分子动力学方面的研究. E-mail:496444091@qq.com
基金资助:
国家自然科学基金资助项目(11505045);河北省自然科学基金资助项目(A2015402035);河北省教育厅资助项目(QN2014134);邯郸市科学技术研究与发展计划项目(1221107079-6;1121103183);邯郸学院课题(15219)

Effects of electrostatic interactions on the movement of kinesin

HUANG Yanbin¹,GUO Haijun¹,LI Jie²,LIU Xiuhong¹,JI Qing³

1.School of Mathematics and Physics, Hebei University of Engineering, Handan 056038, China; 2.School of Mechanical and Electric Engineering, Handan College, Handan 056005, China; 3.Institute of Biophysics, Hebei University of Technology, Tianjin 300401, China

Received:2016-12-10 Online:2017-05-25 Published:2017-05-25

摘要/Abstract

摘要： 利用一种常见驱动蛋白(1BG2)和微管蛋白(1TUB)的结晶结构,通过静电计算得到了马达头部和微管蛋白表面的电势分布,并对比晶体结构分析了微管势场对马达头部正电势区域的作用.此外,利用解泊松方程的方法计算了驱动蛋白与微管间的静电相互作用,并发现马达沿微管轴向运动时所处的微管电势场具有周期性,其周期与马达步进周期有很好的一致性.最后,结合计算结果提出了驱动蛋白在静电作用下的运动机制.

关键词: 驱动蛋白马达, 微管, 静电相互作用, 泊松方程

Abstract: Based on the crystal structure of a kinesin motor(1BG2)and tubulin(1TUB),the electric potential distribution on the surface of the motor head and the tubulin is obtained by electrostatic calculation,and the electrostatic interactions between the microtubule and the positive potential regions of kinesin are analyzed by comparing the crystal structures of them.Furthermore,through simulation by solving Poisson's equation,the electrostatic interactions of kinesin along the microtubule have been calculated,the results show that microtubule provides a periodic potential field for motor movement,and the period is consistent with that of the kinesin steps.Then combined with the calculated results, we present the electrostatic mechanism of kinesin movement.

Key words: kinesin, microtubule, the electrostatic interaction, Poisson's equation.

中图分类号:

Q615

黄艳宾,郭海军,李洁,刘秀红,纪青. 静电相互作用对驱动蛋白马达运动的影响[J]. 河北大学学报(自然科学版), 2017, 37(3): 237-242.

HUANG Yanbin,GUO Haijun,LI Jie,LIU Xiuhong,JI Qing. Effects of electrostatic interactions on the movement of kinesin[J]. Journal of Hebei University (Natural Science Edition), 2017, 37(3): 237-242.

参考文献

[1] HIROKAWA N,NODA Y,TANAKA Y,et al.Kinesin superfamily motor proteins and intracellular transport[J].Nature Reviews Molecular Cell Biology,2009,10(10):682-696.DOI:10.1038/nrm2774.
[2] MORFINI G,SCHMIDT N,WEISSMAN C,et al.Conventional kinesin:Biochemical heterogeneity and functional implications in health and disease[J].Brain Research Bulletin,2016,126:347-353.DOI:10.1016/j.brainresbull.2016.06.009.
[3] HIROKAWA N,TANAKA Y.Kinesin superfamily proteins(KIFs):Various functions and their relevance for important phenomena in life and diseases[J].Experimental Cell Research,2015,334(1):16-25.DOI:10.1016/j.yexcr.2015.02.016.
[4] MYERS S M,COLLINS I.Recent findings and future directions for interpolar mitotic kinesin inhibitors in cancer therapy[J].Future Medicinal Chemistry,2016,8(4):463-489.DOI:10.4155/fmc.16.5.
[5] ISOJIMA H,IINO R,NIITANI Y,et al.Direct observation of intermediate states during the stepping motion of kinesin-1[J].Nature Chemical Biology,2016,12(4):290-297.DOI:10.1038/nchembio.2028.
[6] KANADA R,KUWATA T,KENZAKI H,et al.Structure-based molecular simulations reveal the enhancement of biased brownian motions in single-headed kinesin[J].Plos Computational Biology,2013,9(2):e1002907.DOI:10.1371/journal.pcbi.1002907.
[7] MALEKI M,VASUDEV G,RUEDA L.The role of electrostatic energy in prediction of obligate protein-protein interactions[J].Proteome Science,2013,11(1):1-12.DOI:10.1186/1477-5956-11-S1-S11.
[8] DE JESUS M C,INGLE B L,BARAKAT K A,et al.The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase.[J].The Protein Journal,2014,33(5):403-409.DOI:10.1007/s10930-014-9573-y.
[9] BENMAN H M,WESTBROOK J,FENG Z,et al.The protein data bank[J].Nucleic Acids Research,2000,28(1):235-242.DOI:10.1093/nar/28.1.235.
[10] KULL F J,SABLIN E P,LAU R,et al.Crystal structure of the kinesin motor domain reveals a structural similarity to myosin[J].Nature,1996,380(6574):550-555.DOI:10.1038/380550a0.
[11] NOGALES E,WOLF S G,DOWNING K H.Structure of the alpha beta tubulin dimer by electron crystallography[J].Nature,1998,391(6663):199-203.DOI:10.1038/34465.
[12] KIKKAWA M,HIROKAWA N.High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations[J].Embo Journal,2006,25(18):4187-4194.DOI:10.1038/sj.emboj.7601299.
[13] KIKKAWA M,SABLIN E P,OKADA Y,et al.Switch-based mechanism of kinesin motors[J].Nature,2001,411(6836):439-445.DOI:10.1038/35078000.
[14] BAKER N A,SEPT D,JOSEPH S,et al.Electrostatics of nanosystems:application to microtubules and the ribosome.[J].PNAS,2001,98(18):10037-10041.DOI:10.1073/pnas.181342398.
[15] YAN L.Electrostatic correlations:from plasma to biology[J].Reports on Progress in Physics,2002,65(11):1577-1632.DOI:http://dx.doi.org/10.1088/0034-4885/65/11/201.
[16] ZHANG L Q,BORTHAKUR S,BUCK M.Dissociation of a dynamic protein complex studied by all-atom molecular simulations.[J].Biophysical Journal,2016,110(4):877-886.DOI:10.1016/j.bpj.2015.12.036.
[17] MCCAMMON J A.Darwinian biophysics:Electrostatics and evolution in the kinetics of molecular binding[J].PNAS,2009,106(19):7683-7684.DOI:10.1073/pnas.0902767106.
[18] HIROKAWA N,NITTA R,OKADA Y.The mechanisms of kinesin motor motility:lessons from the monomeric motor KIF1A[J].Nature Reviews Molecular Cell Biology,2009,10(12):877-884.DOI:10.1038/nrm2807.
[19] ATHERTON J,FARABELLA I,YU I M,et al.Conserved mechanisms of microtubule-stimulated ADP release,ATP binding,and force generation in transport kinesins[J].Elife Sciences,2014,3(5):1209-1224.DOI:10.7554/eLife.03680.
[20] ZHENG W J,CHAKRABORTY S.Decrypting the structural,dynamic and energetic basis of kinesin interacting with tubulin dimer in three atpase states by all-atom molecular dynamics simulation[J].Biochemistry,2015,54(3):859-869.DOI:10.1021/bi501056h.
[21] ZHAO Y C,KULL F J,COCHRAN J C.Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding[J].Journal of Biological Chemistry,2010,285(33):25213-25220.DOI:10.1074/jbc.M110.123067.
[22] WANG L,SIU S W,GU W,et al.Downhill binding energy surface of the barnase-barstar complex [J].Biopolymers,2010,93(11):977-985.DOI:10.1002/bip.21507.

静电相互作用对驱动蛋白马达运动的影响

Effects of electrostatic interactions on the movement of kinesin

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