DNA unwinding component of the nonhistone chromatin proteins. Academic Article

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.

authors

• Thomas, Terry

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

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Animals
• Binding Sites
• Chromosomal Proteins, Non-Histone
• DNA
• DNA, Single-Stranded
• DNA, Viral
• Nucleic Acid Conformation
• Poly DA-dT
• Protein Binding
• Rats

PubMed Central ID

• 1069988

Digital Object Identifier (DOI)

• 10.1073/pnas.73.12.4364

start page

• 4364

end page

• 4368

volume

• 73

issue

• 12

URL

• http%3A%2F%2Fdx.doi.org%2F10.1073%2Fpnas.73.12.4364