The dissociation of nuclear proteins from superhelical DNA.

Journal article

Structures retaining many of the morphological features of nuclei may be released by gently lysing human cells in solutions containing non-ionic detergents and high concentrations of salt. These nucleoids contain superhelical DNA. Using a double-labelling procedure we have compared, at different salt concentrations, the amounts and types of protein associated with human nucleoides containings superhelical or relaxed DNA. We find that the slightly lysine-rich histones (H2A and H2B) but not the arginine-rich histones (H3 and H4) dissociate more slowly from nucleoids containing superhelical DNA than from those containing relaxed DNA. A protein of apparent molecular weight of 22000 also binds more tightly to superhelical DNA. We conclude that this protein and the slightly lysine-rich histones transmute free energy of supercoiling into binding energy when they bind to superhelical DNA.

Authors: Levin, J; Jost, E; Cook, P

• Publication status: Published
• Journal: Journal of cell science
• Volume: 29
• Issue: FEB
• Pages: 103-116
• Publication date: 1978-02-01
• EISSN: 1477-9137
• ISSN: 0021-9533
• Language: English
• Keywords: DNA, Superhelical; Lysine; Arginine; Nucleoproteins; Nucleic Acid Conformation; Kinetics; Protein Binding; Molecular Weight; Histones