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Science 13 October 1978:
Vol. 202. no. 4364, pp. 219 - 221
DOI: 10.1126/science.694528

Articles

Science, Vol 202, Issue 4364, 219-221
Copyright © 1978 by American Association for the Advancement of Science


articles

Physiologically important stabilization of DNA by a prokaryotic histone-like protein

DB Stein and DG Searcy

The thermophilic mycoplasma Thermoplasma acidophilum has tightly bound to its DNA a protein that closely resembles the histones of eukaryotes. DNA associated with this protein is more stable than free DNA against thermal denaturation by about 40 degrees C, as shown in both native nucleoprotein and in hybrid nucleoprotein reconstituted in vitro with calf DNA. Since only about 20 percent of the DNA in this organism is associated with the histone-like protein, we suggest that its physiological function is to prevent complete separation of the DNA strands during brief exposures of the organism to denaturing conditions, and thus to facilitate rapid renaturation when normal environmental conditions return.





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Science. ISSN 0036-8075 (print), 1095-9203 (online)