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PMID: 694528 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Science (New York, N.Y.) ·Vol. 202 ·No. 4364 ·1978-10-13 ·Pages 219-21

Stein DB, Searcy DG

Abstract

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.

MeSH Terms
Bacterial Proteins/physiology Biological Evolution DNA Histones/physiology Hot Temperature Nucleic Acid Denaturation Protein Binding Thermoplasma/physiology
Chemicals
Bacterial Proteins Histones DNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Stein D B
Searcy D G
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1978-10-13
Pages
219-21
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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