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Nucleic Acids Research, 1983, Vol. 11, No. 12 4035-4047
© 1983

MOLECULAR BIOLOGY

A destabilized DNA conformation associated with tightly bound nuclear proteins in active genes of rat myoblast

S.A. Leibovitch, M.P. Leibovitch+, J. Hillion, J. Kruh+ and J. Harel

Laboratoire de Biologie Moléculaire CNRS Gr No. 8, Institut Gustave-Roussy, 94800 Villejuif +Institut de Pathologie et Biologie Cellulaire et Moléculaire CNRS, LA 85, INSERM, U.137, Universite Paris V, 24, Rue du Faubourg Saint-Jacques, 75014 Paris, France

Received March 22, 1983. Revised May 23, 1983. Accepted May 23, 1983.

Purified nuclei from tissue cultured myoblasts were disrupted and centrifuqed to equilibrium in a sarcosyl-caesium chloride gradient. A small portion (1.3 % - 1.9%) of the non histone proteins (NHP) were banded with DNA in a hiqh density region of the qradient. The DNA tightly bound to proteins representing about 0.6% of the total nuclear DNA was degraded after treating cell nuclei with S1, nuclease or DNAse I but resisted to mild micrococcal nuclease digestion. A large portion of the DNA sequences complementary to homologous RNA was concentrated in this DNA-proteins fraction. These finding suggest that a subset of NHP strongly associated to the active DNA regions play a role in the destabilisation of the double helical DNA during transcriptional processes.


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