Pf1噬菌体复制 - 组装复合体。高湿度形态的X射线纤维衍射。

Pf1 bacteriophage replication--assembly complex. X-ray fibre diffraction of the high humidity form.

作者信息

Kneale G G, Marvin D A

出版信息

J Mol Biol. 1983 Dec 5;171(2):229-32. doi: 10.1016/s0022-2836(83)80356-8.

Abstract

The helical intracellular nucleoprotein complex of Pf1 bacteriophage has been studied by X-ray fibre diffraction in various hydration states. The helix pitch changes from 44 A in dry fibres to 55 A in wet fibres, whereas the unit rise between subunits in the helix apparently does not change with humidity. This result indicates that the nucleoprotein assembly twists more readily than it stretches. This is consistent with its biological role of tightening the viral DNA into a more compact form for packaging in the virion.

摘要

Pf1噬菌体的螺旋状细胞内核蛋白复合体已通过X射线纤维衍射在不同水合状态下进行了研究。螺旋螺距从干燥纤维中的44埃变为潮湿纤维中的55埃，而螺旋中亚基之间的单位上升显然不会随湿度变化。这一结果表明，核蛋白组装体更容易发生扭曲而非伸展。这与其将病毒DNA收紧成更紧密形式以便包装进病毒粒子的生物学作用是一致的。