Thomas, Terry L. and Patel, Gordhan L. (1976) DNA unwinding component of the nonhistone chromatin proteins. Proceedings of the National Academy of Sciences of the United States of America, 73 (12). pp. 4364-4368. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:THOpnas76
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A subclass of nonhistone chromatin proteins from rat liver, previously shown to exhibit high affinity for DNA, has been fractionated by single-stranded DNA-agarose affinity chromatography. The protein fraction that bound to DNA-agarose in 0.19 M NaCl-buffer and was eluted with 2 M NaCl-buffer is enriched for a protein component of approximately 20,000 daltons and exhibits preferential binding to denatured DNA. This nonhistone protein fraction specific for single strands binds to DNA in a non-species-specific manner, and causes helix-coil transition of synthetic poly[d(A-T)· d(A-T)] at 25 degrees, as indicated by the increase in absorbance of ultraviolet light at 260 nm. The observed hyperchromicity does not result from any nuclease activity in the protein fraction, because addition of Mg+2 results in partial hypochromic shift, and the protein/DNA complex is retained by nitrocellulose filters.
|Additional Information:||© 1976 by the National Academy of Sciences. Communicated by Norman H. Giles, September 7, 1976. This work was supported by U.S. Energy Research and Development Administration Contract no. E (38-1) 644. We thank W. S. Champney, P. Stambrook, and R. Mural for helpful comments on this manuscript.|
|Subject Keywords:||rat liver; DNA affinity chromatography; non-species-specific interaction; preferential A-T binding|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||12 Oct 2007|
|Last Modified:||26 Dec 2012 09:44|
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