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与小鼠微小病毒DNA共价结合的一种蛋白质的鉴定与特性分析。

Identification and characterization of a protein covalently bound to DNA of minute virus of mice.

作者信息

Chow M, Bodnar J W, Polvino-Bodnar M, Ward D C

出版信息

J Virol. 1986 Mar;57(3):1094-104. doi: 10.1128/JVI.57.3.1094-1104.1986.

Abstract

We identified a protein which is covalently linked to a fraction of the DNA synthesized in cells infected with minute virus of mice. This protein is specifically bound to the 5' terminus of the extended terminal conformers of the minute virus of mice replicative-form DNA species and of a variable fraction of single-stranded viral DNA. The chemical stability of the protein-DNA linkage is characteristic of a phosphodiester bond between a tyrosine residue in the protein and the 5' end of the DNA. The terminal protein (TP) bound on all DNA forms has a relative molecular weight of 60,000; it is also seen free in extracts from infected cells. Immunologic comparison of the TP with the other known viral proteins suggests that the TP is not related to the capsid proteins or NS-1.

摘要

我们鉴定出一种蛋白质,它与感染小鼠微小病毒的细胞中合成的一部分DNA共价相连。这种蛋白质特异性地结合于小鼠微小病毒复制型DNA物种的延伸末端构象体的5'末端以及可变比例的单链病毒DNA。蛋白质-DNA连接的化学稳定性是蛋白质中酪氨酸残基与DNA 5'端之间磷酸二酯键的特征。结合在所有DNA形式上的末端蛋白(TP)的相对分子量为60,000;在感染细胞的提取物中也可看到游离的TP。TP与其他已知病毒蛋白的免疫学比较表明,TP与衣壳蛋白或NS-1无关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4fb6/252843/e5cd32f0b7c0/jvirol00114-0392-a.jpg

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