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病毒包装马达对 DNA 的压缩作用：对停滞在衣壳-门复合结构上的 Y 型 DNA 底物的压缩。

DNA crunching by a viral packaging motor: Compression of a procapsid-portal stalled Y-DNA substrate.

机构信息

Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD 21201, USA.

出版信息

Virology. 2010 Mar 15;398(2):224-32. doi: 10.1016/j.virol.2009.11.047. Epub 2010 Jan 12.

DOI:10.1016/j.virol.2009.11.047
PMID:20060554
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2824061/
Abstract

Many large double-stranded DNA viruses employ high force-generating ATP-driven molecular motors to package to high density their genomes into empty procapsids. Bacteriophage T4 DNA translocation is driven by a two-component motor consisting of the procapsid portal docked with a packaging terminase-ATPase. Fluorescence resonance energy transfer and fluorescence correlation spectroscopic (FRET-FCS) studies of a branched (Y-junction) DNA substrate with a procapsid-anchoring leader segment and a single dye molecule situated at the junction point reveal that the "Y-DNA" stalls in proximity to the procapsid portal fused to GFP. Comparable structure Y-DNA substrates containing energy transfer dye pairs in the Y-stem separated by 10 or 14 base pairs reveal that B-form DNA is locally compressed 22-24% by the linear force of the packaging motor. Torsional compression of duplex DNA is thus implicated in the mechanism of DNA translocation.

摘要

许多大型双链 DNA 病毒利用高产生力的 ATP 驱动的分子马达，将其基因组高度浓缩到空的原衣壳中。噬菌体 T4 DNA 转位由一个由两个组件组成的马达驱动，该马达由一个与包装终止酶-ATP 酶对接的原衣壳门组成。带有原衣壳附着的引导片段和一个位于连接点的单个染料分子的分支（Y 型接头）DNA 底物的荧光共振能量转移和荧光相关光谱（FRET-FCS）研究表明，“Y-DNA”在靠近融合到 GFP 的原衣壳门的位置停止。类似的结构 Y-DNA 底物在 Y 干中包含能量转移染料对，它们之间相隔 10 或 14 个碱基对，这表明包装马达的线性力使 B 型 DNA 在局部被压缩 22-24%。因此，双链 DNA 的扭转压缩被牵连到 DNA 转位的机制中。

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