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Nucleic Acids Research, 1980, Vol. 8, No. 12 2577-2590
© 1980

Articles

HMG proteins (1+2) form beaded structures when complexed with closed circulac DNA

D.J. Mathis, A. Kindelis and C. Spadafora

Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Unité 184 de Biologie Moléculaire et de Génie Génétique de I'INSERM, Institut de Chimie Biologique, Faculté de Médecine, Strasbourg France

Received May 16, 1980. Structures bearing a resemblance to nucleosomes can be assembled by incubating calf thymus High Mobility Group proteins (1+2) with closed circular DNA. These HMG proteins are capable of forming beads and inducing superhelicity when bound to DNA. However, they do not protect from nuclease digestion the discrete DNA fragments characteristic of nucleosomes. The relationship between HMGs (1+2) and the "primitive" histone-like DNA-packaging proteins from prokaryotes and mitochondria is discussed.


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