DNA unwinding component of the nonhistone chromatin proteins. Academic Article uri icon


  • 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.

published proceedings

  • Proc Natl Acad Sci U S A

author list (cited authors)

  • Thomas, T. L., & Patel, G. L.

citation count

  • 15

complete list of authors

  • Thomas, TL||Patel, GL

publication date

  • December 1976