Kasamatsu, Harumi and Wu, Madeline (1976) Structure of a nicked DNA-protein complex isolated from simian virus 40: Covalent attachment of the protein to DNA and nick specificity. Proceedings of the National Academy of Sciences of the United States of America, 73 (6). pp. 1945-1949. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:KASpnas76
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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.
|Additional Information:||Copyright © 1976 by the National Academy of Sciences. Communicated by Jerome Vinograd, April 5, 1976. We are indebted to Profs. J. Vinograd and N. Davidson, in whose laboratories this work was conducted, for advice, encouragement, and criticism. This research has been supported by National Institutes of Health Grants CA08014, GM20927, and GM10991.|
|Subject Keywords:||protein-DNA bonding; electron microscopy; iodination of proteins|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||23 Oct 2007|
|Last Modified:||26 Dec 2012 09:45|
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