Molecular assembly and structure of the bacteriophage T4 tail

被引:23
作者
Arisaka F. [1 ]
Yap M.L. [2 ]
Kanamaru S. [3 ]
Rossmann M.G. [2 ]
机构
[1] Life Science Research Center, School of Bioresource Science, Nihon University, 1866 Kameino, Fujisawa
[2] Department of Biological Sciences, Purdue University, West Lafayette, 47907, IN
[3] Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259, Nagatsuta, Midori-ku, Yokohama
基金
美国国家卫生研究院; 日本学术振兴会;
关键词
Assembly; Bacteriophage; Contractile tail; Infection; Molecular recognition; Tail baseplate;
D O I
10.1007/s12551-016-0230-x
中图分类号
学科分类号
摘要
The tail of bacteriophage T4 undergoes large structural changes upon infection while delivering the phage genome into the host cell. The baseplate is located at the distal end of the contractile tail and plays a central role in transmitting the signal to the tail sheath that the tailfibers have been adsorbed by a host bacterium. This then triggers the sheath contraction. In order to understand the mechanism of assembly and conformational changes of the baseplate upon infection, we have determined the structure of an in vitro assembled baseplate through the three-dimensional reconstruction of cryo-electron microscopy images to a resolution of 3.8 Å from electron micrographs. The atomic structure was fitted to the baseplate structure before and after sheath contraction in order to elucidate the conformational changes that occur after bacteriophage T4 has attached itself to a cell surface. The structure was also used to investigate the protease digestion of the assembly intermediates and the mutation sites of the tail genes, resulting in a number of phenotypes. © 2016, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg.
引用
收藏
页码:385 / 396
页数:11
相关论文
共 52 条
[1]  
Abuladze N.K., Gingery M., Tsai I., Eiserling F.A., Tail length determination in bacteriophage T4, Virology, 199, pp. 301-310, (1994)
[2]  
Akhter T., Zhao L., Kohda A., Mio K., Kanamaru S., Arisaka F., The neck of bacteriophage T4 is a ring-like structure formed by a hetero-oligomer of gp13 and gp14, Biochim Biophys Acta, 1774, 8, pp. 1036-1043, (2007)
[3]  
Aksyuk A.A., Leiman P.G., Kurochkina L.P., Schneider M.M., Kostyuchenko V.A., Mesyanzhinov V.V., Rossmann M.G., The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria, EMBO J, 28, pp. 821-829, (2009)
[4]  
Arisaka F., Tschopp J., van Driel R., Engel J., Reassembly of the bacteriophage T4 tail from the core­baseplate and the monomeric sheath protein P18: a cooperative association process, J Mol Biol, 132, pp. 369-386, (1979)
[5]  
Arisaka F., Engel J., Klump J., Contraction and dissociation of the bacteriophage T4 tail sheath induced by heat and urea, Bacteriophage assembly, pp. 365-379, (1981)
[6]  
Brenner S., Horne R.W., A negative staining method for high resolution electron microscopy of viruses, Biochim Biophys Acta, 34, pp. 103-110, (1959)
[7]  
Caspar D.L.D., Movement and self-control in protein assemblies. Quasi-equivalence revisited, Biophys J, 32, (1980)
[8]  
Coombs D.H., Arisaka F., T4 tail structure and function, Molecular biology of bacteriophage T4, pp. 259-281, (1994)
[9]  
Coombs D.H., Eiserling F.A., Studies on the structure, protein composition and assembly of the neck of bacteriophage T4, J Mol Biol, 116, 3, pp. 375-405, (1977)
[10]  
Crowther R.A., Lenk E.V., Kikuchi Y., King J., Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4, J Mol Biol, 116, pp. 489-523, (1977)