COMPARISON OF THE INTERACTIONS OF THE ADENOVIRUS TYPE-2 MAJOR CORE PROTEIN AND ITS PRECURSOR WITH DNA
COMPARISON OF THE INTERACTIONS OF THE ADENOVIRUS TYPE-2 MAJOR CORE PROTEIN AND ITS PRECURSOR WITH DNA
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DOI：
10.1093/nar/14.6.2721
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发表时间：
1986-03-25
影响因子：
14.9
通讯作者：
FLINT, SJ
中科院分区：
文献类型：
--
作者：
CHATTERJEE, PK;YANG, UC;FLINT, SJ
研究了腺病毒2型（Ad2）蛋白VII的主要核心蛋白及其前体蛋白pre-VII与病毒DHA的相互作用，采用紫外诱导32p标记的ollgonuoleotldes与这些蛋白交联。这两种蛋白的蛋白水解片段与dna结合donalns相连，通过它们的同价连接，耐碱32p放射性被鉴定出来。在39°C下组装的H2ts1病毒粒子中，蛋白pre-VII与DHA的整体链结效率与Ad2病毒粒子中蛋白Til与DHA的链结效率相当。然而，包含蛋白前vii的h端一半的蛋白酶T8片段与DHA的连接效率至少是相应的蛋白Til的b端片段的10倍，该片段在病毒粒子饱和期间被蛋白前vii的h端上的23个氨基添加物截断。
The interactions of the major core protein of adenovirus type 2 (Ad2) protein VII, and its precursor, protein pre-VII, with viral DHA, were studied using UV light induoed crossllnklng of32P-labelled ollgonuoleotldes to the proteins. Proteolytio fragments of these two proteins that oontaln DNA-bindlng donalns were Identified by virtue of their oovalently attaohed, alkali-resistant32P-radioaotivity. The overall effioienoy of orossllnking of protein pre-VII to DHA, in H2ts1 virions assembled at 39°C, was comparable to that of the orosslinklng of protein Til to DHA in Ad2 virions. However, a protease T8 fragment comprising the H-terminal half of protein pre-VII orosslinked to DHA at least ten tines Bore efficiently than the corresponding B-termlnal fragnent of protein Til, whlob is truncated by the reaoval of 23 amino adds fron the H-temlnus of protein pre-VII during virion saturation.