Structure of a nicked DNA-protein complex isolated from simian virus 40: covalent attachment of the protein to DNA and nick specificity.
Structure of a nicked DNA-protein complex isolated from simian virus 40: covalent attachment of the protein to DNA and nick specificity.
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从猿猴病毒 40 中分离出的带切口的 DNA-蛋白质复合物的结构：蛋白质与 DNA 的共价连接和切口特异性。
DOI：
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发表时间：
1976
影响因子：
11.1
通讯作者：
M. Wu
中科院分区：
文献类型：
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作者：
H. Kasamatsu;M. Wu
从纯化的猴病毒40中分离到的缺口环状DNA的一部分含有蛋白质-DNA复合体，其中蛋白质(S)共价连接到DNA单链的末端。(缺口DNA是至少含有一个单链断裂的双链DNA。)在电子显微镜下观察该蛋白，并在体外用125I标记。在碱性、4M盐酸胍、3.86M羟胺(pH 4，23)和98%的甲酰胺中，蛋白质与DNA的结合是稳定的。有缺口的环状DNA片段中的大多数分子都含有一个缺口。缺口发生在两条互补的链上；两条链上的特定缺口位置是交错的，但彼此位于数百个核苷酸范围内。
A portion of the nicked circular DNA isolated from purified simian virus 40 contains a protein-DNA complex in which protein(s) is covalently attached to the end of a DNA single strand. (Nicked DNA is double-stranded DNA that contains at least one single-strand scission.) The protein was visualized by electron microscopy and labeled in vitro with 125I. The bond between the protein and the DNA is stable in alkali, 4 M guanidine-hydrochloride, 3.86 M hydroxylamine (pH 4,23), and in 98% formamide. Most of the molecules in the nicked circular DNA fraction contained one nick. The nick occurs on either of the two complementary strands; the specific nick sites on the two strands are staggered, but lie within a few hundred nucleotides of each other.