DNA unwinding component of the nonhistone chromatin proteins
- Creators
- Thomas, Terry L.
- Patel, Gordhan L.
Abstract
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.Files
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Additional details
- Eprint ID
- 8990
- Resolver ID
- CaltechAUTHORS:THOpnas76
- Created
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2007-10-12Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field