DNA poised for release in bacteriophage φ29

被引:79
作者
Tang, Jinghua [3 ]
Olson, Norman [3 ]
Jardine, Paul J. [1 ,2 ]
Grimes, Shelley [1 ,2 ]
Anderson, Dwight L. [1 ,2 ,4 ]
Baker, Timothy S. [3 ,5 ]
机构
[1] Univ Minnesota, Dept Diagnost & Biol Sci, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Inst Mol Virol, Minneapolis, MN 55455 USA
[3] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
[4] Univ Minnesota, Dept Microbiol, Minneapolis, MN 55455 USA
[5] Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA
关键词
D O I
10.1016/j.str.2008.02.024
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We present here the first asymmetric, three-dimensional reconstruction of a tailed dsDNA virus, the mature bacteriophage phi 29, at subnanometer resolution. This structure reveals the rich detail of the asymmetric interactions and conformational dynamics of the phi 29 protein and DNA components, and provides novel insight into the mechanics of virus assembly' For example, the dodecameric head-tail connector protein undergoes significant rearrangement upon assembly into the virion. Specific interactions occur between the tightly packed dsDNA and the proteins of the head and tail. Of particular interest and novelty, an similar to 60 angstrom diameter toroid of dsDNA was observed in the connector-lower collar cavity. The extreme deformation that occurs over a small stretch of DNA is likely a consequence of the high pressure of the packaged genome. This toroid structure may help retain the DNA inside the capsid prior to its injection into the bacterial host.
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页码:935 / 943
页数:9
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