Isolation and Characterization of a Portal Protein-DNA Complex from dsDNA Bacteriophage
作者:
Arthur Zachary,
Lindsay W. Black,
期刊:
Intervirology
(Karger Available online 1992)
卷期:
Volume 33,
issue 1
页码: 6-16
ISSN:0300-5526
年代: 1992
DOI:10.1159/000150225
出版商: S. Karger AG
关键词: Portal protein;DNA packaging;DNA-protein complex;Virus structure
数据来源: Karger
摘要:
A portal protein-DNA complex was isolated from bacteriophage disrupted in 70% acetic acid. This treatment dissociated most of the phage structural proteins, while the portal protein ring remained attached to the highly condensed naked DNA. In the absence of a headful of DNA, the portal ring was not protected. Purification of the portal ring-DNA complex by density gradient centrifugation showed that a dsDNA fragment of about 40 bp was protected from DNase digestion by this association, suggesting it was internalized within the 140 A long, 20^10 Å in diameter T4 apical channel of the ring dodecamer. A portal ring-DNA complex could be isolated from a number of phages (T4, T7, Phi29), and the end(s) of phage T7 DNA was (were) found to be preferentially associated with the ring complex
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