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Volume 270, Number 11, Issue of March 17, 1995 pp. 6286-6291
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Conformational Changes of DNA Minicircles upon the Binding of the Archaebacterial Histone-like Protein MC1

(Received for publication, September 20, 1994; and in revised form, December 6, 1994)

Francine Toulmé ,  Eric Le Cam ,  Caroline Teyssier ,  Etienne Delain ,  Pierre Sautière ,  Jean-Claude Maurizot ,  Françoise Culard

Binding of the archaebacterial histone-like protein MC1 to DNA minicircles has been examined by gel retardation and electron microscopy. MC1 preferentially binds to a 207-base pair relaxed DNA minicircle as compared with the linear fragment. Random binding is observed at very low ionic strength, and a slight increase in salt concentration highly favors the formation of a complex that corresponds to the binding of two MC1 molecules per DNA ring. Measurements of dissociation rates show that this complex is remarkably stable, and electron microscopy reveals that it is characterized by two diametrically opposed kinks. These results are discussed in regard to the mechanisms by which MC1 affects DNA structure.



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[Abstract] [Full Text] [PDF]


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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.