DNA unwinding component of the nonhistone chromatin proteins.
AUTOR(ES)
Thomas, T L
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=431456Documentos Relacionados
- DNA sequence selection by tightly-bound nonhistone chromosomal proteins.
- Identification of nonhistone chromatin proteins in chromatin subunits.
- Effect of non-histone proteins on thermal transition of chromatin and of DNA.
- DNA-binding activity of tightly-bound nonhistone chromosomal proteins in chicken liver chromatin.
- Nonhistone Proteins Control Gene Expression in Reconstituted Chromatin
