文章基本信息

标题：Properties of the Escherichia coli DNA Binding (Unwinding) Protein: Interaction with DNA Polymerase and DNA
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作者：Ian J. Molineux ; Malcolm L. Gefter
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：10
页码：3858-3862
DOI：10.1073/pnas.71.10.3858
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The E. coli DNA binding protein reduces the activity of the single-strand-specific nucleases associated with all three DNA polymerases known in E. coli. A slight excess of binding protein over that required to saturate the DNA template leads to total inhibition of activity of the 3' [->] 5' nucleases associated with DNA polymerases I and III, but restores maximum activity of the DNA polymerase II-associated nuclease. The binding protein forms a specific complex with DNA polymerase II in the absence of DNA, and it is this complex that degrades a DNA{middle dot}binding protein complex. Binding protein also facilitates the binding of DNA polymerase II to single-stranded DNA, whereas the binding to DNA of DNA polymerase I is inhibited. These data may explain the specificity with which the binding protein enhances the synthetic ability of DNA polymerase II.
关键词：single-strand-specific nuclease ; protein·protein and DNA·protein interactions