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Nucleic Acids Research, 1977, Vol. 4, No. 6 1911-1932
© 1977

Articles

Conformational states of chromatin v bodies induced by urea

Donald E. Olins, Philip N. Bryan, Rodney E. Harrington*, Walter E. Hill{dagger} and Ada L. Olins

The University of Tennessee-Oak Ridge Graduate School of Biomedical Sciences,Oak Ridge National Laboratory Oak Ridge, TN 37830, USA the Biology Division, Oak Ridge National Laboratory Oak Ridge, TN 37830, USA

Received March 15, 1977.

Monomer chromatin nu bodies (v1) from chicken erythrocyte nuclei were exposed to 0–10 M urea plus 0.2 mM EDTA (pH 7). Alterations in v1 conformation were examined using hydrodynamic methods (i.e., S,{eta}, and Formula ), thermal denaturation, circular dichroism, reactivity of histone thiol groups to N-ethyl maleimide, and electron microscopy. The two domains of av body (i.e., the DNA-rich shell and the protein-rich core) appeared to respond differently to the destabilizing effects of increasing urea: DNA conformation and stability exhibited noncooperative changes; the core protein structure revealed cooperative destabilization between 4 and 7 M urea. Companion studies on the conformation of the inner histone "heterotypic tetramer" also revealed cooperative destabilization with increasing urea concentration.

*On leave from the Department of Chemistry, University of Nevada, Reno,Nevada 89507.

{dagger}Department of Chemistry, University of Montana, Missoula, Montana 59801.


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[Abstract] [PDF]


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