Purification of the c-fos enhancer-binding protein.

AUTOR(ES)

Prywes, R

RESUMO

We have purified the c-fos enhancer-binding protein from HeLa cell nuclear extracts. The key purification steps involved chromatography on a nonspecific DNA affinity column, from which binding activity and other protein were eluted at low salt concentrations, followed by chromatography on a specific oligonucleotide affinity column, from which the enhancer binding activity was specifically eluted at high salt concentrations. The purified protein had a strong affinity for the c-fos enhancer dyad symmetry sequence, with an equilibrium dissociation constant of 3.3 x 10(-11) M. This affinity was at least 50,000-fold stronger than that found for nonspecific DNA sequences.

Documentos Relacionados

• New B-lymphocyte-specific enhancer-binding protein.
• Induction of apoptosis by c-Fos protein.
• Serum stimulation of the c-fos enhancer induces reversible changes in c-fos chromatin structure.
• The E2 "gene" of bovine papillomavirus encodes an enhancer-binding protein.
• Purification and characterization of the stage-specific embryonic enhancer-binding protein SSAP-1.